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Conserved domains on  [gi|522145229|ref|WP_020656437|]
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bacterioferritin [Massilia niastensis]

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 6.47e-83

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: 240.53  E-value: 6.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   2 KGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGE 81
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522145229  82 STQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQM 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 6.47e-83

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: 240.53  E-value: 6.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   2 KGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGE 81
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522145229  82 STQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQM 154
Cdd:cd00907   81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 1.83e-82

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 239.33  E-value: 1.83e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   3 GDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGES 82
Cdd:COG2193    1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522145229  83 TQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQM 154
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-156 1.80e-70

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: 209.28  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229    1 MKGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229   81 ESTQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQMGE 156
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSE 156
PRK10635 PRK10635
bacterioferritin; Provisional
 1-156 3.39e-65

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 196.21  E-value: 3.39e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   1 MKGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229  81 ESTQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQMGE 156
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKV 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-141 1.27e-37

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: 125.48  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229    8 IRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGE-----S 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 522145229   83 TQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLI 141
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKL 139
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 6.47e-83

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: 240.53  E-value: 6.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   2 KGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGE 81
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522145229  82 STQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQM 154
Cdd:cd00907   81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 1.83e-82

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 239.33  E-value: 1.83e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   3 GDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGES 82
Cdd:COG2193    1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522145229  83 TQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQM 154
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-156 1.80e-70

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: 209.28  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229    1 MKGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229   81 ESTQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQMGE 156
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSE 156
PRK10635 PRK10635
bacterioferritin; Provisional
 1-156 3.39e-65

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 196.21  E-value: 3.39e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   1 MKGDPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229  81 ESTQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLIVKVGIQNYLQSQMGE 156
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKV 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-141 1.27e-37

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: 125.48  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229    8 IRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIGE-----S 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 522145229   83 TQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLI 141
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKL 139
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 3.19e-12

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 59.82  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   9 RLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDEsigEMKHADKLIDRILMLDGLPNLQALHKLLIGESTQ---- 84
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADE---ERRHADALAERLRELGGTPPLPPAHLLAAYALPKtsdd 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229  85 --EMLECDLKLERAAQVTVKEgiaAAEVAADYVTRDLFLEILEDTEEHIEWLETQL 138
Cdd:cd00657   78 paEALRAALEVEARAIAAYRE---LIEQADDPELRRLLERILADEQRHAAWFRKLL 130
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 7-138 1.04e-10

DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a phylogenetically distinct class within the ferritin-like superfamily, and similar in many ways to the DPS (DNA Protecting protein under Starved conditions) proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize hydrogen peroxide in the controlled oxidation of iron, and possess a short N-terminal extension implicated in stabilizing cellular DNA. This domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins are distantly related to bacterial ferritins which assemble 24 monomers, each of which have a four-helix bundle with a fifth shorter helix at the C terminus and a diiron (ferroxidase) center. Ferritins contain a center where oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of iron in the ferric form. Many of the conserved residues of a diiron center are present in this domain.


Pssm-ID: 153111  Cd Length: 148  Bit Score: 56.14  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   7 IIRLLNAQLTNELTAINQYFLHARMYRhwGFERLGKKEY--DESIGEMKHADKLIDRILMLDGLP--NLQALHKLLIGE- 81
Cdd:cd01052    7 LIELLNKAFADEWLAYYYYTILAKHVK--GPEGEGIKEEleEAAEEELNHAELLAERIYELGGTPprDPKDWYEISGCKc 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522145229  82 --------STQEMLECDLKLERAAQVTVKEgIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQL 138
Cdd:cd01052   85 gylppdppDVKGILKVNLKAERCAIKVYKE-LCDMTHGKDPVTYDLALAILNEEIEHEEDLEELL 148
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 7-141 1.69e-09

Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, recombination and repair];


Pssm-ID: 441962  Cd Length: 165  Bit Score: 53.37  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   7 IIRLLNAQLTNELTAINQYFLhARMYRHwGFERLGKKEY--DESIGEMKHADKLIDRILMLDGLP--------NLQALHK 76
Cdd:COG2406   17 LIELLNKAYADEWLAYYYYWI-GAKNVK-GLMGEGIKEEleDHAEEELNHAELLAERIYELGGTPpldpeewaELSGCGY 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522145229  77 LLIGEST--QEMLECDLKLERAAQVTVKEgIAAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLI 141
Cdd:COG2406   95 DLPEDPTdvRAILEQNLKAERCAIKVYNE-LCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGDL 160
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 18-138 5.36e-08

Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153117  Cd Length: 154  Bit Score: 49.20  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229  18 ELTAINQYFlharmYRHWGFErlgkKEYDE--------SIGEMKHADKLIDRILMLDGLPNLQALHK----------LLI 79
Cdd:cd07908   28 ELTAISQYI-----YQHLISE----EKYPEiaetflgiAIVEMHHLEILGQLIVLLGGDPRYRSSSSdkftywtgkyVNY 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522145229  80 GESTQEMLECDLKLERAAQVTVKEgiaAAEVAADYVTRDLFLEILEDTEEHIEWLETQL 138
Cdd:cd07908   99 GESIKEMLKLDIASEKAAIAKYKR---QAETIKDPYIRALLNRIILDEKLHIKILEELL 154
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 52-131 5.69e-05

DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.


Pssm-ID: 153102  Cd Length: 139  Bit Score: 40.61  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229  52 MKHADKLID----RILMLDGLP--NLQALHKL-------LIGESTQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRD 118
Cdd:cd01043   40 YDELREAIDeiaeRIRALGGKPlgTLKEYAELstikeepAGVLSAKEMVAELLEDYETLIEELREAIELADEAGDPATAD 119

                         90
                 ....*....|...
gi 522145229 119 LFLEILEDTEEHI 131
Cdd:cd01043  120 LLTEIIRELEKQA 132
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
6-141 7.85e-05

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 40.48  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   6 NIIRLLNAQLTNELTAINQYflharmyrhwgfERLGKKEYDESIG---------EMKHADKLIDRILMLDG--------- 67
Cdd:COG1633    1 SLLEILKEAIAMEEEAIEFY------------LELAEKAKDPELKklfeelaeeEKKHAELLEKLYEKLGGkpvappeee 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522145229  68 -LPNLQALHKLLIGE-STQEMLECDLKLERAAQVTVKEgiaAAEVAADYVTRDLFLEILEDTEEHIEWLETQLDLI 141
Cdd:COG1633   69 sQPGLAELMDKLDGSvSDAEALELAIATEKDAIEFYRE---LAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 4-129 1.35e-03

nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite.


Pssm-ID: 153113  Cd Length: 156  Bit Score: 37.08  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522145229   4 DPNIIRLLNAQLTNELTAINQYFLHARMYRHWGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHKLLIG-ES 82
Cdd:cd01055    1 SEKLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEfES 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 522145229  83 TQEMLECDLKLERAAQVTVKEGIAAAEVAADYVTRDlFLE--ILEDTEE 129
Cdd:cd01055   81 LLEVFEAALEHEQKVTESINNLVDLALEEKDYATFN-FLQwfVKEQVEE 128
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
4-76 2.96e-03

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 36.26  E-value: 2.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522145229   4 DPNIIRLLNAQLTNELTAINQYF-LHARMYRHwGFERLGKKEYDESIGEMKHADKLIDRILMLDGLPNLQALHK 76
Cdd:COG1528    3 SEKMEKALNEQINLEFYSSYLYLaMAAWCDEK-GLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDA 75
 
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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