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Conserved domains on  [gi|1818940487]
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Chain A, DNA translocase coupling protein

Protein Classification

FtsK/SpoIIIE domain-containing protein( domain architecture ID 1000772)

FtsK/SpoIIIE domain-containing protein similar to Clostridium perfringens DNA translocase coupling protein and Bacillus subtilis spoIIIEA protein

Gene Ontology:  GO:0005524|GO:0003677|GO:0015616
PubMed:  25732341
SCOP:  4000350

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsK super family cl34334
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
112-298 1.75e-35

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1674:

Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 136.59  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 112 VVVGQTFSGNIKI-DLNKSPHILSAGETGSGKSVILRCILWQLLkqgaiaY----------MVDFKGgVEFGLeYEK--- 177
Cdd:COG1674   263 IALGKDISGEPVVaDLAKMPHLLIAGATGSGKSVCINAMILSLL------YkatpdevrliLIDPKM-VELSV-YNGiph 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 178 -VGQVITEVDAAEKLFKYLVDENAKRLKLLRESGSKNIGEYNKKFEGEELK-----------RIIVVIDELAELMDKTGV 245
Cdd:COG1674   335 lLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKgeeeegleplpYIVVIIDELADLMMVAGK 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1818940487 246 DdetraklvrIEGYTSTLARLSRATGINLCIGVQRPDAKVITGQIKNNVPVRI 298
Cdd:COG1674   415 E---------VEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRI 458
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
112-298 1.75e-35

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: 136.59  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 112 VVVGQTFSGNIKI-DLNKSPHILSAGETGSGKSVILRCILWQLLkqgaiaY----------MVDFKGgVEFGLeYEK--- 177
Cdd:COG1674   263 IALGKDISGEPVVaDLAKMPHLLIAGATGSGKSVCINAMILSLL------YkatpdevrliLIDPKM-VELSV-YNGiph 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 178 -VGQVITEVDAAEKLFKYLVDENAKRLKLLRESGSKNIGEYNKKFEGEELK-----------RIIVVIDELAELMDKTGV 245
Cdd:COG1674   335 lLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKgeeeegleplpYIVVIIDELADLMMVAGK 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1818940487 246 DdetraklvrIEGYTSTLARLSRATGINLCIGVQRPDAKVITGQIKNNVPVRI 298
Cdd:COG1674   415 E---------VEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRI 458
PRK10263 PRK10263
DNA translocase FtsK; Provisional
112-320 6.63e-26

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 109.40  E-value: 6.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  112 VVVGQTFSGN-IKIDLNKSPHILSAGETGSGKSV----ILRCILWQLLKQGAIAYMVDFKgGVEFGLeYEKVGQVITEV- 185
Cdd:PRK10263   992 VVLGKDIAGEpVVADLAKMPHLLVAGTTGSGKSVgvnaMILSMLYKAQPEDVRFIMIDPK-MLELSV-YEGIPHLLTEVv 1069
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  186 ----DAAEKLfKYLVDENAKRLKLLRESGSKNIGEYNKKFEG--------------------------EELKRIIVVIDE 235
Cdd:PRK10263  1070 tdmkDAANAL-RWCVNEMERRYKLMSALGVRNLAGYNEKIAEadrmmrpipdpywkpgdsmdaqhpvlKKEPYIVVLVDE 1148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  236 LAELMDKTGvddetraklVRIEGYTSTLARLSRATGINLCIGVQRPDAKVITGQIKNNVPVRICGRFADSKASEIVLSNT 315
Cdd:PRK10263  1149 FADLMMTVG---------KKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQA 1219

                   ....*
gi 1818940487  316 KAKDL 320
Cdd:PRK10263  1220 GAESL 1224
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
99-281 7.58e-20

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: 87.05  E-value: 7.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  99 PWDDKYieeQEGVVVVGQTFSGN-IKIDLNKSP-HILSAGETGSGKSVILRCILWQLLKQGAIA----YMVDFKGGvEFG 172
Cdd:pfam01580   9 PFDTDY---SRLPIALGKDISGNpEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEevqlYCIDPKMG-ELS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 173 lEYEKV-----GQVITEVDAAEKLFKYLVDENAKRLKLLRESGSKNIGEYNKKF-------------------------- 221
Cdd:pfam01580  85 -AYEDIphllsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmctagr 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 222 EGEELKRIIVVIDELAELMdKTGVDDETRaklvRIEGYTSTLARLSRATGINLCIGVQRP 281
Cdd:pfam01580 164 WLEILPYLVVIVDERAELR-LAAPKDSEM----RVEDAIVRLAQKGRAAGIHLLLATQRP 218
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
112-342 7.18e-17

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: 81.94  E-value: 7.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 112 VVVGQTFSGN-IKIDLNKS------PHILSAGETGSGKSVILRCILWQLLKQ----GAIAYMVDFKGGVEF-GLE-YEKV 178
Cdd:TIGR03924 411 VPIGVGDDGEpVELDLKESaeggmgPHGLCIGATGSGKSELLRTLVLGLAAThspeQLNLVLVDFKGGATFlGLEgLPHV 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 179 GQVITevDAAEKLfkYLVD--------ENAKRLKLLRESGS-KNIGEYNK-KFEGEELK---RIIVVIDELAELMdktGV 245
Cdd:TIGR03924 491 SAVIT--NLADEA--PLVDrmqdalagEMNRRQELLRAAGNfANVAEYEKaRAAGADLPplpALFVVVDEFSELL---SQ 563
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 246 DDETRAKLVRIegytstlARLSRATGINLCIGVQRPDAKVITGqIKNNVPVRICGRFADSKASEIVLSNTKAKDLPEVKG 325
Cdd:TIGR03924 564 HPDFADLFVAI-------GRLGRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPG 635
                         250
                  ....*....|....*...
gi 1818940487 326 RFLFKLGADT-VQFQAFY 342
Cdd:TIGR03924 636 AGYLKVDTAEpVRFRAAY 653
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
112-298 1.75e-35

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: 136.59  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 112 VVVGQTFSGNIKI-DLNKSPHILSAGETGSGKSVILRCILWQLLkqgaiaY----------MVDFKGgVEFGLeYEK--- 177
Cdd:COG1674   263 IALGKDISGEPVVaDLAKMPHLLIAGATGSGKSVCINAMILSLL------YkatpdevrliLIDPKM-VELSV-YNGiph 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 178 -VGQVITEVDAAEKLFKYLVDENAKRLKLLRESGSKNIGEYNKKFEGEELK-----------RIIVVIDELAELMDKTGV 245
Cdd:COG1674   335 lLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKgeeeegleplpYIVVIIDELADLMMVAGK 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1818940487 246 DdetraklvrIEGYTSTLARLSRATGINLCIGVQRPDAKVITGQIKNNVPVRI 298
Cdd:COG1674   415 E---------VEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRI 458
PRK10263 PRK10263
DNA translocase FtsK; Provisional
112-320 6.63e-26

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 109.40  E-value: 6.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  112 VVVGQTFSGN-IKIDLNKSPHILSAGETGSGKSV----ILRCILWQLLKQGAIAYMVDFKgGVEFGLeYEKVGQVITEV- 185
Cdd:PRK10263   992 VVLGKDIAGEpVVADLAKMPHLLVAGTTGSGKSVgvnaMILSMLYKAQPEDVRFIMIDPK-MLELSV-YEGIPHLLTEVv 1069
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  186 ----DAAEKLfKYLVDENAKRLKLLRESGSKNIGEYNKKFEG--------------------------EELKRIIVVIDE 235
Cdd:PRK10263  1070 tdmkDAANAL-RWCVNEMERRYKLMSALGVRNLAGYNEKIAEadrmmrpipdpywkpgdsmdaqhpvlKKEPYIVVLVDE 1148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  236 LAELMDKTGvddetraklVRIEGYTSTLARLSRATGINLCIGVQRPDAKVITGQIKNNVPVRICGRFADSKASEIVLSNT 315
Cdd:PRK10263  1149 FADLMMTVG---------KKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQA 1219

                   ....*
gi 1818940487  316 KAKDL 320
Cdd:PRK10263  1220 GAESL 1224
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
99-281 7.58e-20

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: 87.05  E-value: 7.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  99 PWDDKYieeQEGVVVVGQTFSGN-IKIDLNKSP-HILSAGETGSGKSVILRCILWQLLKQGAIA----YMVDFKGGvEFG 172
Cdd:pfam01580   9 PFDTDY---SRLPIALGKDISGNpEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEevqlYCIDPKMG-ELS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 173 lEYEKV-----GQVITEVDAAEKLFKYLVDENAKRLKLLRESGSKNIGEYNKKF-------------------------- 221
Cdd:pfam01580  85 -AYEDIphllsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmctagr 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 222 EGEELKRIIVVIDELAELMdKTGVDDETRaklvRIEGYTSTLARLSRATGINLCIGVQRP 281
Cdd:pfam01580 164 WLEILPYLVVIVDERAELR-LAAPKDSEM----RVEDAIVRLAQKGRAAGIHLLLATQRP 218
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
112-342 7.18e-17

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: 81.94  E-value: 7.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 112 VVVGQTFSGN-IKIDLNKS------PHILSAGETGSGKSVILRCILWQLLKQ----GAIAYMVDFKGGVEF-GLE-YEKV 178
Cdd:TIGR03924 411 VPIGVGDDGEpVELDLKESaeggmgPHGLCIGATGSGKSELLRTLVLGLAAThspeQLNLVLVDFKGGATFlGLEgLPHV 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 179 GQVITevDAAEKLfkYLVD--------ENAKRLKLLRESGS-KNIGEYNK-KFEGEELK---RIIVVIDELAELMdktGV 245
Cdd:TIGR03924 491 SAVIT--NLADEA--PLVDrmqdalagEMNRRQELLRAAGNfANVAEYEKaRAAGADLPplpALFVVVDEFSELL---SQ 563
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 246 DDETRAKLVRIegytstlARLSRATGINLCIGVQRPDAKVITGqIKNNVPVRICGRFADSKASEIVLSNTKAKDLPEVKG 325
Cdd:TIGR03924 564 HPDFADLFVAI-------GRLGRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPG 635
                         250
                  ....*....|....*...
gi 1818940487 326 RFLFKLGADT-VQFQAFY 342
Cdd:TIGR03924 636 AGYLKVDTAEpVRFRAAY 653
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
121-331 3.16e-12

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: 68.09  E-value: 3.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  121 NIKIDLNKSPHILSAGETGSGKSVILRCILWQLLKQGAIA----YMVDF-KGGVefgLEYEK---VGQVIT--EVDAAEK 190
Cdd:TIGR03928  802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEqlhfYLFDFgTNGL---LPLKKlphVADYFTldEEEKIEK 878
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  191 LFKYLVDENAKRLKLLRESGSKNIGEYNKKfEGEELKRIIVVIDELAELMDKTGVDDETRAkLVRIegytstlARLSRAT 270
Cdd:TIGR03928  879 LIRRIKKEIDRRKKLFSEYGVASISMYNKA-SGEKLPQIVIIIDNYDAVKEEPFYEDFEEL-LIQL-------AREGASL 949
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1818940487  271 GINLCIGVQRPDAkvITGQIKNNVPVRICGRFADSKASEIVLSNTKAKdLPEVKGRFLFKL 331
Cdd:TIGR03928  950 GIYLVMTAGRQNA--VRMPLMNNIKTKIALYLIDKSEYRSIVGRTKFT-IEEIPGRGLIKK 1007
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
130-336 2.51e-10

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 62.31  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  130 PHILSAGETGSGKSVILRCILWQLlkqgAIAY--------MVDFKGGvefGLE--YEK----VGqVITEVDAAEKLfKYL 195
Cdd:TIGR03928  470 PHGLVAGTTGSGKSEILQTYILSL----AVNFhphevaflLIDYKGG---GMAnlFKNlphlLG-TITNLDGAQSM-RAL 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  196 VDENA---KRLKLLRESGSKNIGEYNKKF-EG---EELKRIIVVIDELAELMDKtgvDDETRAKLVriegytSTlARLSR 268
Cdd:TIGR03928  541 ASIKAelkKRQRLFGENNVNHINQYQKLYkQGkakEPMPHLFLISDEFAELKSE---QPEFMKELV------ST-ARIGR 610
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1818940487  269 ATGINLCIGVQRPdAKVITGQIKNNVPVRICGRFADSKASEIVLSNTKAKDLpEVKGRFLFKLGADTV 336
Cdd:TIGR03928  611 SLGVHLILATQKP-SGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEI-TVPGRAYLQVGNNEV 676
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
105-255 1.83e-06

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: 49.22  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 105 IEEQEGVVVVGQTFSGN--IKIDLNK--SPHILSAGETGSGKSVILRCILWQLLKQGAIAYMVDFKGgvEF------GLE 174
Cdd:COG0433    19 LLGDGGGILIGKLLSPGvpVYLDLDKllNRHILILGATGSGKSNTLQVLLEELSRAGVPVLVFDPHG--EYsglaepGAE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 175 YEKVGQVITEVDAAEKLFKYLVDENAKRLK-LLRESGSKN----------IGEYNKKFEGEE-LKRIIVVIDELAELMDK 242
Cdd:COG0433    97 RADVGVFDPGAGRPLPINPWDLFATASELGpLLLSRLDLNdtqrgvlreaLRLADDKGLLLLdLKDLIALLEEGEELGEE 176
                         170
                  ....*....|....
gi 1818940487 243 TG-VDDETRAKLVR 255
Cdd:COG0433   177 YGnVSAASAGALLR 190
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
98-243 4.71e-05

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 45.32  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  98 LPWDDKYIEEQEGVVVVGQTFSGNIKIDL---NKSPHILSAGETGSGKSVILRCILWQLLKQGAIAYMVDFKGgvefglE 174
Cdd:COG3451   170 FPFHSFELGDPWGIYLLNTRSGTPVFFDFhdgLDNGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVIFDPGG------S 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 175 YEKV-----GQVITeVDAAEKL----FkYLVDENAKR------LKLLresgsknIGEYNKKFEGEELKRIIVVIDELAEL 239
Cdd:COG3451   244 YEILvralgGTYID-LSPGSPTglnpF-DLEDTEEKRdfllelLELL-------LGREGEPLTPEERAAIDRAVRALYRR 314

                  ....
gi 1818940487 240 MDKT 243
Cdd:COG3451   315 ADPE 318
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
122-256 3.33e-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: 42.67  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487  122 IKIDLNKSPHILSAGETGSGKSVILRCILWQLLKQGAIA-YMVDFKGGVEFGLEYEK-VGQVITEVDAAEKLFKYLVDEN 199
Cdd:TIGR03928 1089 VYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQEKEKiGLIDSIDRGLLAYRDLKeVATYIEEKEDLKEILAELKEEI 1168
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1818940487  200 AKRLKLLRESGSKNIGEYNKkfegeelKRIIVVIDELAELMDKTgvDDETRAKLVRI 256
Cdd:TIGR03928 1169 ELREAAYKEALQNETGEPAF-------KPILLIIDDLEDFIQRT--DLEIQDILALI 1216
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
105-241 1.17e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.16  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818940487 105 IEEQEGVVVVgqtfsgnikidlnksphilsAGETGSGKSVILRCILWQLLKQGAIAYMVDFKGGV---------EFGLEY 175
Cdd:COG3267    39 LAQGGGFVVL--------------------TGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQLSPaellraiadELGLEP 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1818940487 176 EKvgqvITEVDAAEKLFKYLVDENAKRlkllresgsknigeynkkfegeelKRIIVVIDElAELMD 241
Cdd:COG3267    99 KG----ASKADLLRQLQEFLLELAAAG------------------------RRVVLIIDE-AQNLP 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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