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Conserved domains on  [gi|90111193|ref|NP_415466|]
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cell division protein ZapC [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

cell division protein ZapC( domain architecture ID 10537340)

cell division protein ZapC contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ; it acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZapC pfam07126
Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in ...
 2-167 2.06e-88

Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in bacteria. Formation of the Z ring on the cytoplasmic surface of the membrane is the starting process for assembly of the cell-division apparatus. It binds directly to the Z ring, and although it is not essential for absolute cell division it contributes to it by enhancing the interactions between the FtsZ protofilaments (or polymers) which aggregate to form the ring conformation in the Z ring.


:

Pssm-ID: 429305  Cd Length: 169  Bit Score: 255.99  E-value: 2.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193     2 RIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNA 81
Cdd:pfam07126   1 MLKPDDNWRWYFDEEHDRLMLDLGDDMVFRTPYKAKMLIPDAFKESEFSVDDAALYFTFLEKLRELPLSDPQRVQLALNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193    82 LVAIRYLKPQMPKSWHFVSHGEMWVPMPGDaaCVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAG-RAMQLGDAIKI 160
Cdd:pfam07126  81 LAAHRFLKPQMPKSWFFETQAGCVYPELGD--LVQLSNEKERAKFLVVENGENASLCMLLSEQLQLSDsKTLVQFDAIKV 158


                  ....*..
gi 90111193   161 MNDRLKP 167
Cdd:pfam07126 159 MNDRLHP 165
 
Name Accession Description Interval E-value
ZapC pfam07126
Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in ...
 2-167 2.06e-88

Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in bacteria. Formation of the Z ring on the cytoplasmic surface of the membrane is the starting process for assembly of the cell-division apparatus. It binds directly to the Z ring, and although it is not essential for absolute cell division it contributes to it by enhancing the interactions between the FtsZ protofilaments (or polymers) which aggregate to form the ring conformation in the Z ring.


Pssm-ID: 429305  Cd Length: 169  Bit Score: 255.99  E-value: 2.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193     2 RIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNA 81
Cdd:pfam07126   1 MLKPDDNWRWYFDEEHDRLMLDLGDDMVFRTPYKAKMLIPDAFKESEFSVDDAALYFTFLEKLRELPLSDPQRVQLALNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193    82 LVAIRYLKPQMPKSWHFVSHGEMWVPMPGDaaCVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAG-RAMQLGDAIKI 160
Cdd:pfam07126  81 LAAHRFLKPQMPKSWFFETQAGCVYPELGD--LVQLSNEKERAKFLVVENGENASLCMLLSEQLQLSDsKTLVQFDAIKV 158


                  ....*..
gi 90111193   161 MNDRLKP 167
Cdd:pfam07126 159 MNDRLHP 165
 
Name Accession Description Interval E-value
ZapC pfam07126
Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in ...
 2-167 2.06e-88

Cell-division protein ZapC; ZapC is one of four FtsZ-binding components of the Z ring in bacteria. Formation of the Z ring on the cytoplasmic surface of the membrane is the starting process for assembly of the cell-division apparatus. It binds directly to the Z ring, and although it is not essential for absolute cell division it contributes to it by enhancing the interactions between the FtsZ protofilaments (or polymers) which aggregate to form the ring conformation in the Z ring.


Pssm-ID: 429305  Cd Length: 169  Bit Score: 255.99  E-value: 2.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193     2 RIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNA 81
Cdd:pfam07126   1 MLKPDDNWRWYFDEEHDRLMLDLGDDMVFRTPYKAKMLIPDAFKESEFSVDDAALYFTFLEKLRELPLSDPQRVQLALNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111193    82 LVAIRYLKPQMPKSWHFVSHGEMWVPMPGDaaCVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAG-RAMQLGDAIKI 160
Cdd:pfam07126  81 LAAHRFLKPQMPKSWFFETQAGCVYPELGD--LVQLSNEKERAKFLVVENGENASLCMLLSEQLQLSDsKTLVQFDAIKV 158


                  ....*..
gi 90111193   161 MNDRLKP 167
Cdd:pfam07126 159 MNDRLHP 165
 
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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