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Conserved domains on  [gi|1230543584|gb|OYL10834|]
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cell division protein SepF [Streptococcus pneumoniae K2557]

Protein Classification

cell division protein SepF( domain architecture ID 10004532)

cell division protein SepF assembles into large protein rings which bundle FtsZ protofilaments that assemble into a Z ring, which acts as a scaffold for cell division proteins; SepF also anchors the Z ring to the cell membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SepF COG1799
Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, ...
 7-164 1.82e-27

Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 441404 [Multi-domain]  Cd Length: 142  Bit Score: 100.31  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230543584   7 FDRFIDYFT-EDEDSSLPYEKRDEPVFTPVNSSQepalpmnqpsqsagtKENNITRLHARQQELAnqsqratdKVIidVR 85
Cdd:COG1799     4 FDKLKNFFGlEDEEEYEEYEEPEEEEPAPAKPAK---------------KKANVVPLHSATSSQS--------KIV--VV 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1230543584  86 YPRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIVNVEDIRLPDED 164
Cdd:COG1799    59 EPRSYEDAQEIADHLRNGKPVIVNLERMDDDQAKRIVDFLSGLVYALDGSIQKVGNKIFLLTPSNVEVSGEIKEELAEK 137
 
Name Accession Description Interval E-value
SepF COG1799
Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, ...
 7-164 1.82e-27

Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441404 [Multi-domain]  Cd Length: 142  Bit Score: 100.31  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230543584   7 FDRFIDYFT-EDEDSSLPYEKRDEPVFTPVNSSQepalpmnqpsqsagtKENNITRLHARQQELAnqsqratdKVIidVR 85
Cdd:COG1799     4 FDKLKNFFGlEDEEEYEEYEEPEEEEPAPAKPAK---------------KKANVVPLHSATSSQS--------KIV--VV 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1230543584  86 YPRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIVNVEDIRLPDED 164
Cdd:COG1799    59 EPRSYEDAQEIADHLRNGKPVIVNLERMDDDQAKRIVDFLSGLVYALDGSIQKVGNKIFLLTPSNVEVSGEIKEELAEK 137
SepF pfam04472
Cell division protein SepF; SepF accumulates at the cell division site in an FtsZ-dependent ...
 87-153 1.49e-15

Cell division protein SepF; SepF accumulates at the cell division site in an FtsZ-dependent manner and is required for proper septum formation. Mutants are viable but the formation of the septum is much slower and occurs with a very abnormal morphology. This family also includes archaeal related proteins of unknown function.


Pssm-ID: 461323  Cd Length: 72  Bit Score: 67.44  E-value: 1.49e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230543584  87 PRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIV 153
Cdd:pfam04472   6 PRSFEDAQEIADALKNGKIVILNLEGLDKEDAQRIVDFLSGAVYALDGDIQRVGNKIFLLTPSNVDI 72
 
Name Accession Description Interval E-value
SepF COG1799
Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, ...
 7-164 1.82e-27

Cell division protein SepF/YlmF, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441404 [Multi-domain]  Cd Length: 142  Bit Score: 100.31  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230543584   7 FDRFIDYFT-EDEDSSLPYEKRDEPVFTPVNSSQepalpmnqpsqsagtKENNITRLHARQQELAnqsqratdKVIidVR 85
Cdd:COG1799     4 FDKLKNFFGlEDEEEYEEYEEPEEEEPAPAKPAK---------------KKANVVPLHSATSSQS--------KIV--VV 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1230543584  86 YPRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIVNVEDIRLPDED 164
Cdd:COG1799    59 EPRSYEDAQEIADHLRNGKPVIVNLERMDDDQAKRIVDFLSGLVYALDGSIQKVGNKIFLLTPSNVEVSGEIKEELAEK 137
SepF pfam04472
Cell division protein SepF; SepF accumulates at the cell division site in an FtsZ-dependent ...
 87-153 1.49e-15

Cell division protein SepF; SepF accumulates at the cell division site in an FtsZ-dependent manner and is required for proper septum formation. Mutants are viable but the formation of the septum is much slower and occurs with a very abnormal morphology. This family also includes archaeal related proteins of unknown function.


Pssm-ID: 461323  Cd Length: 72  Bit Score: 67.44  E-value: 1.49e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230543584  87 PRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIV 153
Cdd:pfam04472   6 PRSFEDAQEIADALKNGKIVILNLEGLDKEDAQRIVDFLSGAVYALDGDIQRVGNKIFLLTPSNVDI 72
 
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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