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Conserved domains on  [gi|1251777357|gb|ATI12547|]
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bacterioferritin [Acetobacter pomorum]

Protein Classification

bacterioferritin( domain architecture ID 10005564)

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
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
4-154 2.25e-78

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


:

Pssm-ID: 441796  Cd Length: 152  Bit Score: 229.31  E-value: 2.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   4 DPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQDV 83
Cdd:COG2193     2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGEDV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  84 KEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQLNS 154
Cdd:COG2193    82 EEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
4-154 2.25e-78

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 229.31  E-value: 2.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   4 DPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQDV 83
Cdd:COG2193     2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGEDV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  84 KEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQLNS 154
Cdd:COG2193    82 EEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 3-154 2.52e-78

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: 229.35  E-value: 2.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   3 KDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQD 82
Cdd:cd00907     2 GDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGED 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251777357  83 VKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQLNS 154
Cdd:cd00907    82 VPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-151 2.63e-61

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: 186.55  E-value: 2.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   1 MVKDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  81 QDVKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQ 151
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQ 151
PRK10635 PRK10635
bacterioferritin; Provisional
 1-151 1.50e-56

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 174.25  E-value: 1.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   1 MVKDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  81 QDVKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQ 151
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQ 151
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 1.16e-34

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: 118.16  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   8 IEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQ-----D 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  83 VKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQ 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
7-130 1.46e-03

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 37.24  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   7 VIEHLNIQLTNELTAINQYFLHartlrHWGVT---------LLGkkEYEESIEEmrHADWLIERILYLGGLP-----NVQ 72
Cdd:NF041388   24 IVDALNTDLAATYVLYHQLKKH-----HWNVEgaefrdlhlFLG--EAAEDAEE--AADELAERAQALGGVPvsgpaALE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251777357  73 RLNTILI-GQDVKEI---LECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEH 130
Cdd:NF041388   95 EHAPVEPeGEDVYDIrtsLENDLEMYGDIIESVRDHIELAENLGDHATAELLREQLVELEED 156
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
4-154 2.25e-78

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 229.31  E-value: 2.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   4 DPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQDV 83
Cdd:COG2193     2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGEDV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  84 KEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQLNS 154
Cdd:COG2193    82 EEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 3-154 2.52e-78

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: 229.35  E-value: 2.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   3 KDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQD 82
Cdd:cd00907     2 GDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGED 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251777357  83 VKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQLNS 154
Cdd:cd00907    82 VPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-151 2.63e-61

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: 186.55  E-value: 2.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   1 MVKDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  81 QDVKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQ 151
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQ 151
PRK10635 PRK10635
bacterioferritin; Provisional
 1-151 1.50e-56

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 174.25  E-value: 1.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   1 MVKDPKVIEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  81 QDVKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQIGIERYIQ 151
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQ 151
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 1.16e-34

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: 118.16  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   8 IEHLNIQLTNELTAINQYFLHARTLRHWGVTLLGKKEYEESIEEMRHADWLIERILYLGGLPNVQRLNTILIGQ-----D 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  83 VKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLIKQ 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 11-136 1.84e-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: 60.59  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357  11 LNIQLTNELTAINQYFLHARTLRHWGVtllgKKEYEESI-EEMRHADWLIERILYLGGLPNVQRLN------TILIGQDV 83
Cdd:cd00657     3 LNDALAGEYAAIIAYGQLAARAPDPDL----KDELLEIAdEERRHADALAERLRELGGTPPLPPAHllaayaLPKTSDDP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1251777357  84 KEILECDLKLEEKALGDLREgiaYCESVRDFVSRDLLLKILENEEEHEDFLDR 136
Cdd:cd00657    79 AEALRAALEVEARAIAAYRE---LIEQADDPELRRLLERILADEQRHAAWFRK 128
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 6-135 2.49e-08

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: 49.98  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   6 KVIEHLNIQLTNELTAINQYFLHARTLRhwgvTLLG---KKEYEES-IEEMRHADWLIERILYLGGLP--NVQRLNTILI 79
Cdd:cd01052     6 ELIELLNKAFADEWLAYYYYTILAKHVK----GPEGegiKEELEEAaEEELNHAELLAERIYELGGTPprDPKDWYEISG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251777357  80 ---------GQDVKEILECDLKLEEKALGDLREGIAYCESvRDFVSRDLLLKILENEEEHE-DFLD 135
Cdd:cd01052    82 ckcgylppdPPDVKGILKVNLKAERCAIKVYKELCDMTHG-KDPVTYDLALAILNEEIEHEeDLEE 146
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 6-135 2.25e-07

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 47.59  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   6 KVIEHLNIQLTNELTAINQYFLHARTLRhwGVTLLG-KKEYEES-IEEMRHADWLIERILYLGGLP--NVQRL-NTILIG 80
Cdd:COG2406    16 ELIELLNKAYADEWLAYYYYWIGAKNVK--GLMGEGiKEELEDHaEEELNHAELLAERIYELGGTPplDPEEWaELSGCG 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251777357  81 Q-------DVKEILECDLKLEEKALGDLREGIAYCESVrDFVSRDLLLKILENEEEHE-DFLD 135
Cdd:COG2406    94 YdlpedptDVRAILEQNLKAERCAIKVYNELCNMTKGK-DPVTYDLALDILEEEVEHEqDLED 155
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 18-130 1.27e-06

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: 45.73  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357  18 ELTAINQYFLHartlrHWgvtlLGKKEYEE--------SIEEMRHADWLIERILYLGGLP---NVQRLNTIL-------I 79
Cdd:cd07908    28 ELTAISQYIYQ-----HL----ISEEKYPEiaetflgiAIVEMHHLEILGQLIVLLGGDPryrSSSSDKFTYwtgkyvnY 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1251777357  80 GQDVKEILECDLKLEEKALGDLREGIAYcesVRDFVSRDLLLKILENEEEH 130
Cdd:cd07908    99 GESIKEMLKLDIASEKAAIAKYKRQAET---IKDPYIRALLNRIILDEKLH 146
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 6-134 8.29e-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: 43.28  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   6 KVIEHLNIQLTNELTAINQYFLHartlrHWGVTllGK------KEYEESIEEMR-HADWLIERILYLGGLPN-----VQR 73
Cdd:COG0783    13 KVAEALNQLLADLYVLYLKTKNA-----HWNVK--GPnffslhELFEELYDELReAIDEIAERIRALGGVPPgtlaeFAK 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251777357  74 LNTI----LIGQDVKEILECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILeneEEHEDFL 134
Cdd:COG0783    86 LSTIkeepEGVVDAREMVEALLEDYEALIKTLREAIELADEAGDEGTADLLTDIL---RELEKRA 147
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 34-130 5.68e-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: 37.91  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357  34 HWGVTllGK------KEYEESIEEMR-HADWLIERILYLGGLP-----NVQRLNTI----LIGQDVKEILECDLKLEEKA 97
Cdd:cd01043    21 HWNVK--GPnffalhELFEELYDELReAIDEIAERIRALGGKPlgtlkEYAELSTIkeepAGVLSAKEMVAELLEDYETL 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1251777357  98 LGDLREGIAYCESVRDFVSRDLLLKILENEEEH 130
Cdd:cd01043    99 IEELREAIELADEAGDPATADLLTEIIRELEKQ 131
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
7-130 1.46e-03

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 37.24  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   7 VIEHLNIQLTNELTAINQYFLHartlrHWGVT---------LLGkkEYEESIEEmrHADWLIERILYLGGLP-----NVQ 72
Cdd:NF041388   24 IVDALNTDLAATYVLYHQLKKH-----HWNVEgaefrdlhlFLG--EAAEDAEE--AADELAERAQALGGVPvsgpaALE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251777357  73 RLNTILI-GQDVKEI---LECDLKLEEKALGDLREGIAYCESVRDFVSRDLLLKILENEEEH 130
Cdd:NF041388   95 EHAPVEPeGEDVYDIrtsLENDLEMYGDIIESVRDHIELAENLGDHATAELLREQLVELEED 156
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
6-141 3.62e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 35.85  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251777357   6 KVIEHLNIQLTNELTAINQYFLHARTLRhwgvTLLGKKEYEE-SIEEMRHADWLIERILYLGG----------LPNVQRL 74
Cdd:COG1633     1 SLLEILKEAIAMEEEAIEFYLELAEKAK----DPELKKLFEElAEEEKKHAELLEKLYEKLGGkpvappeeesQPGLAEL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251777357  75 NTILIGQ-DVKEILECDLKLEEKALGDLREgiaYCESVRDFVSRDLLLKILENEEEHEDFLDRQFDLI 141
Cdd:COG1633    77 MDKLDGSvSDAEALELAIATEKDAIEFYRE---LAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 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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