|
Name |
Accession |
Description |
Interval |
E-value |
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
601-913 |
1.29e-46 |
|
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: 179.40 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 601 LCQHADGLSL---EAFCAALENlYRAGCEQEQGALSEGQvhqsahlfSSLQQQNRADDMAVESVLQRWSAQRYASDIRCY 677
Cdd:TIGR03924 342 FGVAPDQLSIaeaEALARRLAR-WRAATAGTVDAPLTGA--------RDLLELLGIGDPATLDVDRLWRPRPGRDRLRVP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 678 LGVSSGGS---LNIGLSEH---GPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKGSAGLGPLAQLPHALS 751
Cdd:TIGR03924 413 IGVGDDGEpveLDLKESAEggmGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLPHVSA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 752 VLSNF--DVSAVERALEFLRADIHRREVDLQALG-VNSYRDYLASCQAAGTTPRYPELLIVVDEFRMLIDSMPDaMAELM 828
Cdd:TIGR03924 493 VITNLadEAPLVDRMQDALAGEMNRRQELLRAAGnFANVAEYEKARAAGADLPPLPALFVVVDEFSELLSQHPD-FADLF 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 829 -RIATIGRSLGLHLVLATQRPQGAISQDIRANIATSICLRVASAQDSYNLLEHESAAYISaAHPGAGYVRLPDGRSLPFR 907
Cdd:TIGR03924 572 vAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYHLP-STPGAGYLKVDTAEPVRFR 650
|
....*.
gi 283133749 908 APLVDA 913
Cdd:TIGR03924 651 AAYVSG 656
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
690-849 |
3.69e-22 |
|
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: 96.68 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 690 LSEHGPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKGSAgLGPLAQLPHALSVLSNFDVSAVERALEFLR 769
Cdd:pfam01580 34 LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGE-LSAYEDIPHLLSVPVATDPKRALRALEWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 770 ADIHRREVDLQALGVNSYRDY----------------------LASCQAAGTTPRYPELLIVVDEFrmlIDSMPDAMAE- 826
Cdd:pfam01580 113 DEMERRYALFRALGVRSIAGYngeiaedpldgfgdvflviygvHVMCTAGRWLEILPYLVVIVDER---AELRLAAPKDs 189
|
170 180 190
....*....|....*....|....*....|
gi 283133749 827 -------LMRIATIGRSLGLHLVLATQRPQ 849
Cdd:pfam01580 190 emrvedaIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
695-874 |
4.48e-20 |
|
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: 96.53 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 695 PHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKgsagLGPLAQLPHALS-VLSnfDVSAVERALEFLRADIH 773
Cdd:COG1674 282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKmv-eLSVYNGIPHLLTpVVT--DPKKAANALKWAVREME 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 774 RREVDLQALGV---NSYRDYLASCQAAGTTPRYPE----LLIVVDEFrmlidsmpdamAELM------------RIATIG 834
Cdd:COG1674 359 RRYKLFAKAGVrniAGYNEKVREAKAKGEEEEGLEplpyIVVIIDEL-----------ADLMmvagkeveeaiaRLAQKA 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 283133749 835 RSLGLHLVLATQRPqgaiSQD-----IRANIATSICLRVASAQDS 874
Cdd:COG1674 428 RAAGIHLILATQRP----SVDvitglIKANIPSRIAFAVSSKIDS 468
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
695-883 |
8.06e-17 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 87.06 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 695 PHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKgSAGLGPLAQLPHALSVLSNfDVSAVERALEFLRADIHR 774
Cdd:PRK10263 1011 PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHLLTEVVT-DMKDAANALRWCVNEMER 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 775 REVDLQALGVNS---YRDYLASCQAAG-------------------TTPRYPELLIVVDEFRMLIDSMPDAMAELM-RIA 831
Cdd:PRK10263 1089 RYKLMSALGVRNlagYNEKIAEADRMMrpipdpywkpgdsmdaqhpVLKKEPYIVVLVDEFADLMMTVGKKVEELIaRLA 1168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 283133749 832 TIGRSLGLHLVLATQRPQ-GAISQDIRANIATSICLRVASAQDSYNLLEHESA 883
Cdd:PRK10263 1169 QKARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGA 1221
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
124-199 |
3.80e-03 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 38.01 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 124 ILRGPEAGATFPISRGRTSLGRAALparggeqpHHIHLQDPFLKPVHGSFYADSSGIR----------WIEKRPAASEGS 193
Cdd:pfam16697 2 VLSGPHAGAEFPLEGGRYRIGSDPD--------CDIVLSDKEVSRVHLKLEVDDEGWRlddlgsgngtLVNGQRVTELGI 73
|
....*.
gi 283133749 194 EKAHGS 199
Cdd:pfam16697 74 ALRPGD 79
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
601-913 |
1.29e-46 |
|
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: 179.40 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 601 LCQHADGLSL---EAFCAALENlYRAGCEQEQGALSEGQvhqsahlfSSLQQQNRADDMAVESVLQRWSAQRYASDIRCY 677
Cdd:TIGR03924 342 FGVAPDQLSIaeaEALARRLAR-WRAATAGTVDAPLTGA--------RDLLELLGIGDPATLDVDRLWRPRPGRDRLRVP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 678 LGVSSGGS---LNIGLSEH---GPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKGSAGLGPLAQLPHALS 751
Cdd:TIGR03924 413 IGVGDDGEpveLDLKESAEggmGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLPHVSA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 752 VLSNF--DVSAVERALEFLRADIHRREVDLQALG-VNSYRDYLASCQAAGTTPRYPELLIVVDEFRMLIDSMPDaMAELM 828
Cdd:TIGR03924 493 VITNLadEAPLVDRMQDALAGEMNRRQELLRAAGnFANVAEYEKARAAGADLPPLPALFVVVDEFSELLSQHPD-FADLF 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 829 -RIATIGRSLGLHLVLATQRPQGAISQDIRANIATSICLRVASAQDSYNLLEHESAAYISaAHPGAGYVRLPDGRSLPFR 907
Cdd:TIGR03924 572 vAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYHLP-STPGAGYLKVDTAEPVRFR 650
|
....*.
gi 283133749 908 APLVDA 913
Cdd:TIGR03924 651 AAYVSG 656
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
661-896 |
2.65e-45 |
|
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: 179.80 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 661 VLQRWSAQRYASDIRCYLGVSSGG---SLNIGLSEHGPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKGS 737
Cdd:TIGR03928 433 IQERWAKNETYKSLAVPIGLRGKDdivYLNLHEKAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 738 AGLGPLAQLPHALSVLSNFDVSAVERALEFLRADIHRREVDLQALGVNSYRDYLASCQAAGTTPRYPELLIVVDEFRMLI 817
Cdd:TIGR03928 513 GMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAELK 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283133749 818 DSMPDAMAELMRIATIGRSLGLHLVLATQRPQGAISQDIRANIATSICLRVASAQDSYNLLEHESAAYISAahPGAGYV 896
Cdd:TIGR03928 593 SEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITV--PGRAYL 669
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
686-925 |
2.87e-22 |
|
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: 103.15 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 686 LNIGLSEHGPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFkGSAGLGPLAQLPHALSVLSNFDVSAVERAL 765
Cdd:TIGR03925 71 LVVDLSGAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDF-GGGGLASLADLPHVGGVAGRLDPERVRRTV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 766 EFLRADIHRREVDLQALGVNSYRDYLAScQAAGTTPRYP--ELLIVVDEFRMLIDSMPDAMAELMRIATIGRSLGLHLVL 843
Cdd:TIGR03925 150 AEVEGLLRRRERLFRTHGIDSMAQYRAR-RAAGRLPEDPfgDVFLVIDGWGTLRQDFEDLEDKVTDLAARGLAYGVHVVL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 844 ATQRPQGaISQDIRANIATSICLRVASAQDSynLLEHESAAYISAAHPGAGYVrlPDGRSLPFRAPLVDAVPSSSDARPV 923
Cdd:TIGR03925 229 TASRWSE-IRPALRDLIGTRIELRLGDPMDS--EIDRRAAARVPAGRPGRGLT--PDGLHMLIALPRLDGIASVDDLGTR 303
|
..
gi 283133749 924 QV 925
Cdd:TIGR03925 304 GL 305
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
690-849 |
3.69e-22 |
|
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: 96.68 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 690 LSEHGPHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKGSAgLGPLAQLPHALSVLSNFDVSAVERALEFLR 769
Cdd:pfam01580 34 LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGE-LSAYEDIPHLLSVPVATDPKRALRALEWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 770 ADIHRREVDLQALGVNSYRDY----------------------LASCQAAGTTPRYPELLIVVDEFrmlIDSMPDAMAE- 826
Cdd:pfam01580 113 DEMERRYALFRALGVRSIAGYngeiaedpldgfgdvflviygvHVMCTAGRWLEILPYLVVIVDER---AELRLAAPKDs 189
|
170 180 190
....*....|....*....|....*....|
gi 283133749 827 -------LMRIATIGRSLGLHLVLATQRPQ 849
Cdd:pfam01580 190 emrvedaIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
695-874 |
4.48e-20 |
|
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: 96.53 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 695 PHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKgsagLGPLAQLPHALS-VLSnfDVSAVERALEFLRADIH 773
Cdd:COG1674 282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKmv-eLSVYNGIPHLLTpVVT--DPKKAANALKWAVREME 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 774 RREVDLQALGV---NSYRDYLASCQAAGTTPRYPE----LLIVVDEFrmlidsmpdamAELM------------RIATIG 834
Cdd:COG1674 359 RRYKLFAKAGVrniAGYNEKVREAKAKGEEEEGLEplpyIVVIIDEL-----------ADLMmvagkeveeaiaRLAQKA 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 283133749 835 RSLGLHLVLATQRPqgaiSQD-----IRANIATSICLRVASAQDS 874
Cdd:COG1674 428 RAAGIHLILATQRP----SVDvitglIKANIPSRIAFAVSSKIDS 468
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
686-878 |
6.80e-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: 96.98 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 686 LNIGLSEHGpHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFkGSAGLGPLAQLPHALSVLSNFDVSAVERAL 765
Cdd:TIGR03928 803 LTLDLSKDG-HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDF-GTNGLLPLKKLPHVADYFTLDEEEKIEKLI 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 766 EFLRADIHRREVDLQALGVNSYRDYLascQAAGTTprYPELLIVVDEFRMLIDS--MPDAMAELMRIATIGRSLGLHLVL 843
Cdd:TIGR03928 881 RRIKKEIDRRKKLFSEYGVASISMYN---KASGEK--LPQIVIIIDNYDAVKEEpfYEDFEELLIQLAREGASLGIYLVM 955
|
170 180 190
....*....|....*....|....*....|....*
gi 283133749 844 ATQRpQGAISQDIRANIATSICLRVASAQDSYNLL 878
Cdd:TIGR03928 956 TAGR-QNAVRMPLMNNIKTKIALYLIDKSEYRSIV 989
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
695-883 |
8.06e-17 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 87.06 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 695 PHWLLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDFKgSAGLGPLAQLPHALSVLSNfDVSAVERALEFLRADIHR 774
Cdd:PRK10263 1011 PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHLLTEVVT-DMKDAANALRWCVNEMER 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 775 REVDLQALGVNS---YRDYLASCQAAG-------------------TTPRYPELLIVVDEFRMLIDSMPDAMAELM-RIA 831
Cdd:PRK10263 1089 RYKLMSALGVRNlagYNEKIAEADRMMrpipdpywkpgdsmdaqhpVLKKEPYIVVLVDEFADLMMTVGKKVEELIaRLA 1168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 283133749 832 TIGRSLGLHLVLATQRPQ-GAISQDIRANIATSICLRVASAQDSYNLLEHESA 883
Cdd:PRK10263 1169 QKARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGA 1221
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
806-873 |
5.03e-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: 63.47 E-value: 5.03e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283133749 806 LLIVVDEFRMLIDSMPDAMAELM-RIATIGRSLGLHLVLATQRPqGAISQDIRANIATSICLRVASAQD 873
Cdd:COG0433 260 LVLVIDEAHLLAPAAPSALLEILeRIAREGRKFGVGLILATQRP-SDIDEDVLSQLGTQIILRLFNPRD 327
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
682-896 |
7.91e-04 |
|
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: 44.21 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 682 SGGSLNIGLSEH-----------GPHWLLGGTTGAGKSQLLRSLVLSAALRyppERLGLILVDFKGSaGLGPLAQLPHAL 750
Cdd:TIGR03928 1073 EEGSIPIGLDEEtvepvyidlteNPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSIDR-GLLAYRDLKEVA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 751 SVLSNFDvsAVERALEFLRADIHRREVDLQALGVNSYrdylascqaagTTPRYPELLIVVDEF----RMLIDSMPDAMAE 826
Cdd:TIGR03928 1149 TYIEEKE--DLKEILAELKEEIELREAAYKEALQNET-----------GEPAFKPILLIIDDLedfiQRTDLEIQDILAL 1215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283133749 827 LMriaTIGRSLGLHLVLATQ-----RPQGAISQDIRaNIATSICLRVASAQDSYNLLEHESAAYISaahPGAGYV 896
Cdd:TIGR03928 1216 IM---KNGKKLGIHFIVAGThselsKSYDGVPKEIK-QLRTGILGMRKSDQSFFKLPFTRSEKELE---PGEGYF 1283
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
804-889 |
1.14e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 43.05 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 804 PELLIVVDEFRML--IDSMPDAMAElmriatiGRSLGLHLVLATQ-RPQG------AISQDIRANIATSICLRVAsaqds 874
Cdd:COG3505 247 RPVLLLLDEFANLgrLPSLETLLAT-------GRGYGIRLVLILQsLAQLeaiygeEGAETILGNCGTKIFLGVN----- 314
|
90
....*....|....*
gi 283133749 875 ynllEHESAAYISAA 889
Cdd:COG3505 315 ----DPETAEYLSEL 325
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
378-932 |
2.39e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.55 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 378 YLRGRNLPLGALEKQDAPHYLPLPTPVLGHylKLEEAHLRAYLVQLVAGYPGSVHVLLAEAHNSAQKRMNALLQTLAVVP 457
Cdd:COG3321 841 WVAGVPVDWSALYPGRGRRRVPLPTYPFQR--EDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 458 GVSVHCLPGTQQEKYLQALQSSLQSELSSSVPPLILMPQHASAVYAPLLTALTSGAIAEGSQSRALSSPREQKMNAPALC 537
Cdd:COG3321 919 LALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAA 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 538 VLGSAEGDNSAHAPGALFGAAWVECASEGSHRQSIRYRAQGYAMPPVQPTEGVYQVHPLACEGLCQHADGLSLEAFCAAL 617
Cdd:COG3321 999 AAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELA 1078
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 618 EnlyragcEQEQGALSEGQVHQSAHLFSSLQQQNRADDMAVESVLQRWSAQRYASDIRCYLGVSSGGSLNIGLSEHGPHW 697
Cdd:COG3321 1079 L-------AAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALA 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 698 LLGGTTGAGKSQLLRSLVLSAALRYPPERLGLILVDfkGSAGLGPLAQLPHALSVLSNFDVSAVERALEFLRADIHRREV 777
Cdd:COG3321 1152 LAAAAAALAAALAAALLAAAALLLALALALAAALAA--ALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAA 1229
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 778 DLQALGVNSYRDYLASCQAAGTTPRYPELLIVVDEFRMLIDSMPDAMAELMRIATIGRSLGLHLVLATQRPQGAISQDIR 857
Cdd:COG3321 1230 AAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAA 1309
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283133749 858 ANIATSICLRVASAQDSYNLLEHESAAYISAAHPGAGYVRLPDGRSLPFRAPLVDAVPSSSDARPVQVLGLEEGG 932
Cdd:COG3321 1310 AAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
124-199 |
3.80e-03 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 38.01 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283133749 124 ILRGPEAGATFPISRGRTSLGRAALparggeqpHHIHLQDPFLKPVHGSFYADSSGIR----------WIEKRPAASEGS 193
Cdd:pfam16697 2 VLSGPHAGAEFPLEGGRYRIGSDPD--------CDIVLSDKEVSRVHLKLEVDDEGWRlddlgsgngtLVNGQRVTELGI 73
|
....*.
gi 283133749 194 EKAHGS 199
Cdd:pfam16697 74 ALRPGD 79
|
|
|