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Conserved domains on  [gi|1633454]
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Chain V, BACTERIOFERRITIN

Protein Classification

bacterioferritin( domain architecture ID 10793432)

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
PRK10635 PRK10635
bacterioferritin; Provisional
 1-158 1.27e-102

bacterioferritin; Provisional


:

Pssm-ID: 182604  Cd Length: 158  Bit Score: 290.58  E-value: 1.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454     1 MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633454    81 EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG 158
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKVED 158
 
Name Accession Description Interval E-value
PRK10635 PRK10635
bacterioferritin; Provisional
 1-158 1.27e-102

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 290.58  E-value: 1.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454     1 MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633454    81 EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG 158
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKVED 158
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 1.08e-88

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: 255.51  E-value: 1.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454      1 MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1633454     81 EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREE 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 1.37e-87

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: 252.47  E-value: 1.37e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    2 KGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGE 81
Cdd:cd00907   1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633454   82 DVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQI 154
Cdd:cd00907  81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 5.61e-86

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 248.57  E-value: 5.61e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    3 GDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGED 82
Cdd:COG2193   1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633454   83 VEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQI 154
Cdd:COG2193  81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 4.21e-38

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: 126.63  E-value: 4.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454      8 INYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGE-----D 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633454     83 VEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQK 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
 
Name Accession Description Interval E-value
PRK10635 PRK10635
bacterioferritin; Provisional
 1-158 1.27e-102

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 290.58  E-value: 1.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454     1 MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633454    81 EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG 158
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQIKVED 158
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 1.08e-88

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: 255.51  E-value: 1.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454      1 MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1633454     81 EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREE 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 1.37e-87

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: 252.47  E-value: 1.37e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    2 KGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGE 81
Cdd:cd00907   1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633454   82 DVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQI 154
Cdd:cd00907  81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 5.61e-86

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 248.57  E-value: 5.61e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    3 GDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGED 82
Cdd:COG2193   1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633454   83 VEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQI 154
Cdd:COG2193  81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 4.21e-38

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: 126.63  E-value: 4.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454      8 INYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGE-----D 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633454     83 VEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQK 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 6.72e-17

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: 72.14  E-value: 6.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    9 NYLNKLLGNELVAINQYFLHARMFKNWGLKrlNDVEYHESiDEMKHADRYIERILFLEGLP------NLQDLGKLNIGED 82
Cdd:cd00657   1 RLLNDALAGEYAAIIAYGQLAARAPDPDLK--DELLEIAD-EERRHADALAERLRELGGTPplppahLLAAYALPKTSDD 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1633454   83 VEEMLRSDLALELDGAKNLREAIGYADsvhDYVSRDMMIEILRDEEGHIDWLETEL 138
Cdd:cd00657  78 PAEALRAALEVEARAIAAYRELIEQAD---DPELRRLLERILADEQRHAAWFRKLL 130
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 5-128 1.47e-06

DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms];


Pssm-ID: 440546 [Multi-domain]  Cd Length: 156  Bit Score: 45.21  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    5 TKVINYLNKLLGNELVAINQYflharmfKN--WGLKRLNDVEYHESIDEM-----KHADRYIERILFLEGLP--NLQDLG 75
Cdd:COG0783  12 EKVAEALNQLLADLYVLYLKT-------KNahWNVKGPNFFSLHELFEELydelrEAIDEIAERIRALGGVPpgTLAEFA 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454   76 KL-NIGE------DVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEE 128
Cdd:COG0783  85 KLsTIKEepegvvDAREMVEALLEDYEALIKTLREAIELADEAGDEGTADLLTDILRELE 144
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 6-146 3.80e-06

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 44.51  E-value: 3.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    6 KVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLP--NLQDLGKL-NIG-- 80
Cdd:COG2406  16 ELIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPplDPEEWAELsGCGyd 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1633454   81 -----EDVEEMLRSDLALEldgaknlREAIGY----ADSVH--DYVSRDMMIEILRDEEGHIDWLETELDLIQKMGL 146
Cdd:COG2406  96 lpedpTDVRAILEQNLKAE-------RCAIKVynelCNMTKgkDPVTYDLALDILEEEVEHEQDLEDLLGDLESGHF 165
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 18-135 5.84e-05

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: 40.72  E-value: 5.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454   18 ELVAINQYFLHARMFKNWGLKrLNDVEYHESIDEMKHADRYIERILFLEGLPNL----------QDLGKLNIGEDVEEML 87
Cdd:cd07908  28 ELTAISQYIYQHLISEEKYPE-IAETFLGIAIVEMHHLEILGQLIVLLGGDPRYrssssdkftyWTGKYVNYGESIKEML 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 1633454   88 RSDLALELDGAKNLREAIGYADsvhDYVSRDMMIEILRDEEGHIDWLE 135
Cdd:cd07908 107 KLDIASEKAAIAKYKRQAETIK---DPYIRALLNRIILDEKLHIKILE 151
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 6-138 2.36e-04

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: 39.20  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    6 KVINYLNKLLGNELVAINQYFLHARMFKnwGLKRLNDVEYHE--SIDEMKHADRYIERILFLEGLP--NLQDLGKLNIGE 81
Cdd:cd01052   6 ELIELLNKAFADEWLAYYYYTILAKHVK--GPEGEGIKEELEeaAEEELNHAELLAERIYELGGTPprDPKDWYEISGCK 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633454   82 ---------DVEEMLRSDLALELDGAKNLREAIGYADSvHDYVSRDMMIEILRDEEGHIDWLETEL 138
Cdd:cd01052  84 cgylppdppDVKGILKVNLKAERCAIKVYKELCDMTHG-KDPVTYDLALAILNEEIEHEEDLEELL 148
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 44-131 4.50e-04

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: 38.30  E-value: 4.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454   44 EYHESIDEM-KHADRYI----ERILFLEGLP--NLQDLGKLNI-------GEDVEEMLRSDLALELDGAKNLREAIGYAD 109
Cdd:cd01043  31 ALHELFEELyDELREAIdeiaERIRALGGKPlgTLKEYAELSTikeepagVLSAKEMVAELLEDYETLIEELREAIELAD 110

                        90       100
                ....*....|....*....|..
gi 1633454  110 SVHDYVSRDMMIEILRDEEGHI 131
Cdd:cd01043 111 EAGDPATADLLTEIIRELEKQA 132
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
6-141 1.74e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 36.62  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633454    6 KVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLndveYHE-SIDEMKHADRYIERILFLEG----------LPNLQDL 74
Cdd:COG1633   1 SLLEILKEAIAMEEEAIEFYLELAEKAKDPELKKL----FEElAEEEKKHAELLEKLYEKLGGkpvappeeesQPGLAEL 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633454   75 -GKLNIGEDVEEMLRSDLALELDGAKNLREAigyADSVHDYVSRDMMIEILRDEEGHIDWLETELDLI 141
Cdd:COG1633  77 mDKLDGSVSDAEALELAIATEKDAIEFYREL---AAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
 
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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