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Conserved domains on  [gi|1756725689|gb|QFG24436|]
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bacterioferritin [Actinomadura sp. WMMB 499]

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];
35-177 6.05e-31

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


:

Pssm-ID: 441796  Cd Length: 152  Bit Score: 109.51  E-value: 6.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHtqy 114
Cdd:COG2193     3 PKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGE--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756725689 115 ktfkddDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDLMDLLG 177
Cdd:COG2193    80 ------DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLE 137
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
35-177 6.05e-31

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 109.51  E-value: 6.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHtqy 114
Cdd:COG2193     3 PKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGE--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756725689 115 ktfkddDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDLMDLLG 177
Cdd:COG2193    80 ------DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLE 137
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 33-176 5.54e-26

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: 96.59  E-value: 5.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  33 SVEQVISVLNDVVATEvvcWMRYAQHAISA---TGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARR 109
Cdd:cd01052     3 DVDELIELLNKAFADE---WLAYYYYTILAkhvKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756725689 110 SHTQYKTFKDD--DLRGMLEENLVAERIVIESYQEIIRWLGDGDVTTRRLMEDILAEEEEHADDLMDLL 176
Cdd:cd01052    80 SGCKCGYLPPDppDVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEHEEDLEELL 148
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 38-178 2.27e-23

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: 89.65  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  38 ISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIarrsHTQYKTF 117
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVEL----LAIEAPP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756725689 118 KDDDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDLMDLLGK 178
Cdd:pfam00210  77 SFGSVLEVLEAALEHEKKVTKSLRELIELAEEeGDYATADFLQWFLDEQEEHEWFLEALLEK 138
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
35-172 5.65e-08

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 49.95  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLN-DVVATEVVcwmrYAQ---HAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRS 110
Cdd:NF041388   22 EQIVDALNtDLAATYVL----YHQlkkHHWNVEGAEFRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756725689 111 HTqykTFKDDD---LRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDL 172
Cdd:NF041388   98 PV---EPEGEDvydIRTSLENDLEMYGDIIESVRDHIELAENlGDHATAELLREQLVELEEDAHHI 160
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 80-177 4.37e-05

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 42.01  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  80 EERHHAMRAAERISQLGGNPDFDPETIARRSHTQYKTFKDD--DLRGMLEENLVAERIVIESYQEIIRWLGDGDVTTRRL 157
Cdd:PRK13456   64 EDRNHFEALVPRIYELGGKLPRDIREFHDISACPDAYLPENptDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTYDL 143

                          90       100
                  ....*....|....*....|
gi 1756725689 158 MEDILAEEEEHADDLMDLLG 177
Cdd:PRK13456  144 ALAILQEEIEHEAWFSELLG 163
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
35-177 6.05e-31

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 109.51  E-value: 6.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHtqy 114
Cdd:COG2193     3 PKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGE--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756725689 115 ktfkddDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDLMDLLG 177
Cdd:COG2193    80 ------DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLE 137
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 34-178 7.61e-28

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 101.90  E-value: 7.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  34 VEQVISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHTQ 113
Cdd:COG2406    14 VDELIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWAELSGCG 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756725689 114 YKTFKD-DDLRGMLEENLVAERIVIESYQEIIRWLGDGDVTTRRLMEDILAEEEEHADDLMDLLGK 178
Cdd:COG2406    94 YDLPEDpTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGD 159
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 33-176 5.54e-26

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: 96.59  E-value: 5.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  33 SVEQVISVLNDVVATEvvcWMRYAQHAISA---TGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARR 109
Cdd:cd01052     3 DVDELIELLNKAFADE---WLAYYYYTILAkhvKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756725689 110 SHTQYKTFKDD--DLRGMLEENLVAERIVIESYQEIIRWLGDGDVTTRRLMEDILAEEEEHADDLMDLL 176
Cdd:cd01052    80 SGCKCGYLPPDppDVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEHEEDLEELL 148
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 40-176 2.95e-24

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: 91.79  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  40 VLNDVVATEVVCWMRYAQHAISATginRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRshtQYKTFKD 119
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAP---DPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAA---YALPKTS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1756725689 120 DDLRGMLEENLVAERIVIESYQEIIRWLGDGDvtTRRLMEDILAEEEEHADDLMDLL 176
Cdd:cd00657    76 DDPAEALRAALEVEARAIAAYRELIEQADDPE--LRRLLERILADEQRHAAWFRKLL 130
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 38-178 2.27e-23

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: 89.65  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  38 ISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIarrsHTQYKTF 117
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVEL----LAIEAPP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756725689 118 KDDDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDLMDLLGK 178
Cdd:pfam00210  77 SFGSVLEVLEAALEHEKKVTKSLRELIELAEEeGDYATADFLQWFLDEQEEHEWFLEALLEK 138
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 35-177 7.42e-15

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: 67.96  E-value: 7.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLNDVVATEVVCWMRYAQHAISAT--GINRAqvADEFNEHAHEERHHAMRAAERISQLGGNPDfdpetIARRSHT 112
Cdd:cd00907     4 PKVIEALNKALTGELTAINQYFLHARMLEdwGLEKL--AERFRKESIEEMKHADKLIERILFLEGLPN-----LQRLGKL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756725689 113 QYKTfkddDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHAD------DLMDLLG 177
Cdd:cd00907    77 RIGE----DVPEMLENDLALEYEAIAALNEAIALCEEvGDYVSRDLLEEILEDEEEHIDwletqlDLIDKMG 144
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 35-169 6.26e-09

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: 52.14  E-value: 6.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLNDVVATEVVCWMRYAQHAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHTQY 114
Cdd:COG0783    12 EKVAEALNQLLADLYVLYLKTKNAHWNVKGPNFFSLHELFEELYDELREAIDEIAERIRALGGVPPGTLAEFAKLSTIKE 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756725689 115 KTFKDDDLRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHA 169
Cdd:COG0783    92 EPEGVVDAREMVEALLEDYEALIKTLREAIELADEaGDEGTADLLTDILRELEKRA 147
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
37-178 1.69e-08

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 50.88  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  37 VISVLNDVVATEVVCWMRYAQHAISATginRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHTQYKT 116
Cdd:COG1633     2 LLEILKEAIAMEEEAIEFYLELAEKAK---DPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESQPGLAELMD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756725689 117 F--KDDDLRGMLEENLVAERIVIESYQEIIRWLGDGDVttRRLMEDILAEEEEHADDLMDLLGK 178
Cdd:COG1633    79 KldGSVSDAEALELAIATEKDAIEFYRELAAKVGDPEI--KKLFEELAADEKEHAALLEGLYDR 140
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
35-172 5.65e-08

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 49.95  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  35 EQVISVLN-DVVATEVVcwmrYAQ---HAISATGINRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRS 110
Cdd:NF041388   22 EQIVDALNtDLAATYVL----YHQlkkHHWNVEGAEFRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756725689 111 HTqykTFKDDD---LRGMLEENLVAERIVIESYQEIIRWLGD-GDVTTRRLMEDILAEEEEHADDL 172
Cdd:NF041388   98 PV---EPEGEDvydIRTSLENDLEMYGDIIESVRDHIELAENlGDHATAELLREQLVELEEDAHHI 160
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 69-176 2.42e-07

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 47.74  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  69 QVADEFNEHAHEERHHAMRAAERISQLGGNPDFDPETIARRSHTQYKTF--KDDDLRGMLEENLVAERIVIESYQEIIRW 146
Cdd:pfam02915  30 QIAELFEEMAEEERRHAGFLNKLLKDLFPGLELIPLEHVRGYAEFPPKFltTATNLEEAIEGEYAEEEEMYRFYEELAEK 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1756725689 147 LGDGDvtTRRLMEDILAEEEEHADDLMDLL 176
Cdd:pfam02915 110 EGYPE--ARKLFEDLAEAEKRHEERFRKLL 137
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 70-169 7.02e-07

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: 46.38  E-value: 7.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  70 VADEFNEHAHEerhhamrAAERISQLGGNPDFDPETIARRSHTQYKTFKDDDLRGMLEENLVAERIVIESYQEIIRWLGD 149
Cdd:cd01043    39 LYDELREAIDE-------IAERIRALGGKPLGTLKEYAELSTIKEEPAGVLSAKEMVAELLEDYETLIEELREAIELADE 111

                          90       100
                  ....*....|....*....|.
gi 1756725689 150 -GDVTTRRLMEDILAEEEEHA 169
Cdd:cd01043   112 aGDPATADLLTEIIRELEKQA 132
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 55-176 3.34e-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: 44.57  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  55 YAQHAISATGINRaQVADEFNEHAHEERHHAMRAAERISQLGGNPDFdpetiaRRSHTQYKTFKD-------DDLRGMLE 127
Cdd:cd07908    35 YIYQHLISEEKYP-EIAETFLGIAIVEMHHLEILGQLIVLLGGDPRY------RSSSSDKFTYWTgkyvnygESIKEMLK 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1756725689 128 ENLVAERIVIESYQEIIRWLGDGDVttRRLMEDILAEEEEHADDLMDLL 176
Cdd:cd07908   108 LDIASEKAAIAKYKRQAETIKDPYI--RALLNRIILDEKLHIKILEELL 154
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 80-177 4.37e-05

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 42.01  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  80 EERHHAMRAAERISQLGGNPDFDPETIARRSHTQYKTFKDD--DLRGMLEENLVAERIVIESYQEIIRWLGDGDVTTRRL 157
Cdd:PRK13456   64 EDRNHFEALVPRIYELGGKLPRDIREFHDISACPDAYLPENptDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTYDL 143

                          90       100
                  ....*....|....*....|
gi 1756725689 158 MEDILAEEEEHADDLMDLLG 177
Cdd:PRK13456  144 ALAILQEEIEHEAWFSELLG 163
DUF2383 pfam09537
Domain of unknown function (DUF2383); Members of this protein family are found mostly in the ...
 33-145 5.59e-04

Domain of unknown function (DUF2383); Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


Pssm-ID: 430673  Cd Length: 106  Bit Score: 37.58  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756725689  33 SVEQVISVLNDVVATevvcWMRYAQHAisatgiNRAQVADEFNEHAHEERHHAMRAAERISQLGGNPDfDPETIARRSHT 112
Cdd:pfam09537   1 ALNDLIETLYDGEDG----YKTAAENV------KDPQLKTLLQRRAAERRAAARELQSEIRALGGEPE-DGGSFAGTLHR 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1756725689 113 QY----KTFKDDDLRGMLEENLVAERIVIESYQEIIR 145
Cdd:pfam09537  70 AWvdlkSALTSNDEEAILEELERGEDAALEAYEEALE 106
 
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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