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Conserved domains on  [gi|2076832670|gb|QYJ81540|]
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bacterioferritin [Shewanella aegiceratis]

Protein Classification

bacterioferritin( domain architecture ID 10097036)

bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 1.11e-69

Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity.


:

Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   2 KGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGE 81
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076832670  82 NPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQM 154
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 1.11e-69

Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity.


Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   2 KGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGE 81
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076832670  82 NPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQM 154
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 8.73e-67

Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];


Pssm-ID: 441796  Cd Length: 152  Bit Score: 199.65  E-value: 8.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   3 GHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGEN 82
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076832670  83 PEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQM 154
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 1.35e-58

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 179.24  E-value: 1.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   1 MKGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076832670  81 ENPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQMESE 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
PRK10635 PRK10635
bacterioferritin; Provisional
 1-157 1.66e-53

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 166.55  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   1 MKGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076832670  81 ENPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQMESE 157
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKVE 157
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-117 2.39e-27

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 99.28  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   8 IRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGE-----N 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2076832670  83 PEEMLQCDKTMLEEQLVELRSVIALCETERDYVSR 117
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATA 115
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 1.11e-69

Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity.


Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   2 KGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGE 81
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076832670  82 NPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQM 154
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 8.73e-67

Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];


Pssm-ID: 441796  Cd Length: 152  Bit Score: 199.65  E-value: 8.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   3 GHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGEN 82
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076832670  83 PEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQM 154
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 1.35e-58

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 179.24  E-value: 1.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   1 MKGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076832670  81 ENPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQMESE 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
PRK10635 PRK10635
bacterioferritin; Provisional
 1-157 1.66e-53

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 166.55  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   1 MKGHPNVIRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076832670  81 ENPEEMLQCDKTMLEEQLVELRSVIALCETERDYVSREILEDLLEDEEEYLDWIEAQQDLIKMTGIQNYLQSQMESE 157
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKVE 157
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-117 2.39e-27

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 99.28  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076832670   8 IRQLNKILTFELTAINQYFLHARMYKNWGLEELNEKCYKKSIKDMKHADKLIERVLFLEGLPNLQQLEKLRIGE-----N 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2076832670  83 PEEMLQCDKTMLEEQLVELRSVIALCETERDYVSR 117
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATA 115
 
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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