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Conserved domains on  [gi|1815835609|gb|QIE90099|]
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bacterioferritin [Pseudomonas nitroreducens]

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];
32-177 1.23e-36

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


:

Pssm-ID: 441796  Cd Length: 152  Bit Score: 124.15  E-value: 1.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  32 DRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGltersha 111
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLG------- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 112 EYVAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:COG2193    74 KLRIGEDVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLELIE 140
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
32-177 1.23e-36

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 124.15  E-value: 1.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  32 DRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGltersha 111
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLG------- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 112 EYVAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:COG2193    74 KLRIGEDVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLELIE 140
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 38-173 4.78e-25

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: 93.71  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  38 RLLNESLATELVCYLRYKRHYFMAtglKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTeRSHAEYVAGK 117
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARA---PDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLL-AAYALPKTSD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1815835609 118 NLREMITENLVAERIAVDSYREIVVYLgdDDPTTRRLFEEILAQEEEHADDMADLL 173
Cdd:cd00657    77 DPAEALRAALEVEARAIAAYRELIEQA--DDPELRRLLERILADEQRHAAWFRKLL 130
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 39-177 5.50e-21

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: 83.49  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  39 LLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHAEYVagKN 118
Cdd:pfam00210   3 ALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSF--GS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609 119 LREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEeGDYATADFLQWFLDEQEEHEWFLEALLEKLE 140
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 36-167 2.05e-11

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: 59.05  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  36 VLRLLNESLATELVCYLRYKRHYFMAT--GLKAsVAAAEFLEhATQELQHADLLAERIMQLGGEPDFNPAGltershaEY 113
Cdd:TIGR00754   7 VIQHLNKQLTNELTAINQYFLHARMQKnwGLKE-LADHEYHE-SIDEMKHADEIIERILFLEGLPNLQDLG-------KL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1815835609 114 VAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHAD 167
Cdd:TIGR00754  78 RIGETVREMLEADLALELDVLNRLKEAIAYAEEvRDYVSRDLLEEILEDEEEHID 132
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
40-175 1.50e-07

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 48.79  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  40 LNESLATELVCYLRYKRHYFmatglkaSVAAAEFL-------EHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHAE 112
Cdd:NF041388   28 LNTDLAATYVLYHQLKKHHW-------NVEGAEFRdlhlflgEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVE 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1815835609 113 YVAGK--NLREMITENLVAERIAVDSYR---EIVVYLGddDPTTRRLFEEILAQEEEHADDMADLLQD 175
Cdd:NF041388  101 PEGEDvyDIRTSLENDLEMYGDIIESVRdhiELAENLG--DHATAELLREQLVELEEDAHHIEHYLED 166
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 32-165 3.28e-06

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 45.09  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  32 DRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASvAAAEFLEHATQE-LQHADLLAERIMQLGGEPDFNPAGLTERS- 109
Cdd:PRK13456   17 DVDKLVELLVKNAAAEFTTYYYYTILRAHLIGLEGE-GLKEIAEDARLEdRNHFEALVPRIYELGGKLPRDIREFHDISa 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1815835609 110 --HAEYVAGKNLREMITENLV-AERIAVDSYREIVVYLGDDDPTTRRLFEEILAQEEEH 165
Cdd:PRK13456   96 cpDAYLPENPTDPKEILKVLLeAERCAIRTYTEICDMTAGKDPRTYDLALAILQEEIEH 154
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
32-177 1.23e-36

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 124.15  E-value: 1.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  32 DRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGltersha 111
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLG------- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 112 EYVAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:COG2193    74 KLRIGEDVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLELIE 140
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 31-177 1.10e-27

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 101.52  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  31 ADRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTERSH 110
Cdd:COG2406    12 VDVDELIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWAELSG 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609 111 AEYVAGKN---LREMITENLVAERIAVDSYREIVVYLGDDDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:COG2406    92 CGYDLPEDptdVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGDLE 161
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 38-173 4.78e-25

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: 93.71  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  38 RLLNESLATELVCYLRYKRHYFMAtglKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTeRSHAEYVAGK 117
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARA---PDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLL-AAYALPKTSD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1815835609 118 NLREMITENLVAERIAVDSYREIVVYLgdDDPTTRRLFEEILAQEEEHADDMADLL 173
Cdd:cd00657    77 DPAEALRAALEVEARAIAAYRELIEQA--DDPELRRLLERILADEQRHAAWFRKLL 130
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 31-173 2.79e-24

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: 92.35  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  31 ADRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTERSH 110
Cdd:cd01052     2 LDVDELIELLNKAFADEWLAYYYYTILAKHVKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEISG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 111 AEYVA----GKNLREMITENLVAERIAVDSYREIVVYLGDDDPTTRRLFEEILAQEEEHADDMADLL 173
Cdd:cd01052    82 CKCGYlppdPPDVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEHEEDLEELL 148
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 39-177 5.50e-21

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: 83.49  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  39 LLNESLATELVCYLRYKRHYFMATGLKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHAEYVagKN 118
Cdd:pfam00210   3 ALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSF--GS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609 119 LREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHADDMADLLQDLK 177
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEeGDYATADFLQWFLDEQEEHEWFLEALLEKLE 140
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 34-167 2.41e-18

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: 77.20  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  34 KTVLRLLNESLATELVCYLRYKRHYFMAT--GLKAsvAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTErsha 111
Cdd:cd00907     4 PKVIEALNKALTGELTAINQYFLHARMLEdwGLEK--LAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLR---- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 112 eyvAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHAD 167
Cdd:cd00907    78 ---IGEDVPEMLENDLALEYEAIAALNEAIALCEEvGDYVSRDLLEEILEDEEEHID 131
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 36-167 2.05e-11

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: 59.05  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  36 VLRLLNESLATELVCYLRYKRHYFMAT--GLKAsVAAAEFLEhATQELQHADLLAERIMQLGGEPDFNPAGltershaEY 113
Cdd:TIGR00754   7 VIQHLNKQLTNELTAINQYFLHARMQKnwGLKE-LADHEYHE-SIDEMKHADEIIERILFLEGLPNLQDLG-------KL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1815835609 114 VAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHAD 167
Cdd:TIGR00754  78 RIGETVREMLEADLALELDVLNRLKEAIAYAEEvRDYVSRDLLEEILEDEEEHID 132
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 30-166 2.99e-11

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: 58.31  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  30 HADRKTVLRLLNESLATELVCYLRYKRHYFMATGlkasvaaAEFL-------EHATQELQHADLLAERIMQLGGEPDFNP 102
Cdd:COG0783     8 EEAREKVAEALNQLLADLYVLYLKTKNAHWNVKG-------PNFFslhelfeELYDELREAIDEIAERIRALGGVPPGTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 103 AGLTERSH-AEYVAGK-NLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHA 166
Cdd:COG0783    81 AEFAKLSTiKEEPEGVvDAREMVEALLEDYEALIKTLREAIELADEaGDEGTADLLTDILRELEKRA 147
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
35-176 2.28e-09

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 53.19  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  35 TVLRLLNESLATELVCYLRYKRHYFMAtglKASVAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHAEYV 114
Cdd:COG1633     1 SLLEILKEAIAMEEEAIEFYLELAEKA---KDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESQPGLAELM 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1815835609 115 AG----KNLREMITENLVAERIAVDSYREIVVYLgdDDPTTRRLFEEILAQEEEHADDMADLLQDL 176
Cdd:COG1633    78 DKldgsVSDAEALELAIATEKDAIEFYRELAAKV--GDPEIKKLFEELAADEKEHAALLEGLYDRL 141
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
40-175 1.50e-07

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 48.79  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  40 LNESLATELVCYLRYKRHYFmatglkaSVAAAEFL-------EHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHAE 112
Cdd:NF041388   28 LNTDLAATYVLYHQLKKHHW-------NVEGAEFRdlhlflgEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVE 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1815835609 113 YVAGK--NLREMITENLVAERIAVDSYR---EIVVYLGddDPTTRRLFEEILAQEEEHADDMADLLQD 175
Cdd:NF041388  101 PEGEDvyDIRTSLENDLEMYGDIIESVRdhiELAENLG--DHATAELLREQLVELEEDAHHIEHYLED 166
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 39-166 4.08e-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: 46.77  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  39 LLNESLATELVCYLRYKRHYFMATGlkasvaaAEFL-------EHATQELQHADLLAERIMQLGGEPDFNPAGLTERSHA 111
Cdd:cd01043     2 ALNQLLADLYVLYLKLKNYHWNVKG-------PNFFalhelfeELYDELREAIDEIAERIRALGGKPLGTLKEYAELSTI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1815835609 112 EYVAGKNL--REMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHA 166
Cdd:cd01043    75 KEEPAGVLsaKEMVAELLEDYETLIEELREAIELADEaGDPATADLLTEIIRELEKQA 132
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 32-165 3.28e-06

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 45.09  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  32 DRKTVLRLLNESLATELVCYLRYKRHYFMATGLKASvAAAEFLEHATQE-LQHADLLAERIMQLGGEPDFNPAGLTERS- 109
Cdd:PRK13456   17 DVDKLVELLVKNAAAEFTTYYYYTILRAHLIGLEGE-GLKEIAEDARLEdRNHFEALVPRIYELGGKLPRDIREFHDISa 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1815835609 110 --HAEYVAGKNLREMITENLV-AERIAVDSYREIVVYLGDDDPTTRRLFEEILAQEEEH 165
Cdd:PRK13456   96 cpDAYLPENPTDPKEILKVLLeAERCAIRTYTEICDMTAGKDPRTYDLALAILQEEIEH 154
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 73-166 6.67e-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: 43.80  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  73 FLEHATQELQHADLLAERIMQLGGEPDF--NPAGLTERSHAEYVA-GKNLREMITENLVAERIAVDSYREIVVYLgdDDP 149
Cdd:cd07908    53 FLGIAIVEMHHLEILGQLIVLLGGDPRYrsSSSDKFTYWTGKYVNyGESIKEMLKLDIASEKAAIAKYKRQAETI--KDP 130

                          90
                  ....*....|....*..
gi 1815835609 150 TTRRLFEEILAQEEEHA 166
Cdd:cd07908   131 YIRALLNRIILDEKLHI 147
PRK10635 PRK10635
bacterioferritin; Provisional
 34-167 1.14e-05

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 43.28  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  34 KTVLRLLNESLATELVCYLRYKRH--YFMATGLKaSVAAAEFLEhATQELQHADLLAERIMQLGGEPDFNPAGltersha 111
Cdd:PRK10635    5 VKIINYLNKLLGNELVAINQYFLHarMFKNWGLM-RLNDVEYHE-SIDEMKHADKYIERILFLEGIPNLQDLG------- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1815835609 112 EYVAGKNLREMITENLVAERIAVDSYREIVVYLGD-DDPTTRRLFEEILAQEEEHAD 167
Cdd:PRK10635   76 KLNIGEDVEEMLRSDLRLELEGAKDLREAIAYADSvHDYVSRDMMIEILADEEGHID 132
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 39-173 1.01e-04

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 40.42  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815835609  39 LLNESLATELVCYLRYKrhyFMATGLKAS--VAAAEFLEHATQELQHADLLAERIMQLGGEPDFNPA----GLTERSHAE 112
Cdd:pfam02915   2 NLEKAIAGESSARRRYK---ELAEKAKNEypQIAELFEEMAEEERRHAGFLNKLLKDLFPGLELIPLehvrGYAEFPPKF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1815835609 113 YVAGKNLREMITENLVAERIAVDSYREIVVYLGDDDptTRRLFEEILAQEEEHADDMADLL 173
Cdd:pfam02915  79 LTTATNLEEAIEGEYAEEEEMYRFYEELAEKEGYPE--ARKLFEDLAEAEKRHEERFRKLL 137
 
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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