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Conserved domains on  [gi|1421772393|ref|WP_111876212|]
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bacterioferritin [Paracidovorax anthurii]

Protein Classification

bacterioferritin( domain architecture ID 10097036)

bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 6.21e-75

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: 220.50  E-value: 6.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   2 QGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPRE-FTPGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1421772393  81 TVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLrDTEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 6.21e-75

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: 220.50  E-value: 6.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   2 QGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPRE-FTPGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1421772393  81 TVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLrDTEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-153 7.20e-73

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 215.44  E-value: 7.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   3 GNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPR-EFTPGTT 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLgKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421772393  82 VPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQ 151
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-153 1.24e-41

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: 136.48  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   1 MQGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDM-RPREFTPG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421772393  80 TTVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDTEEdHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQ 153
PRK10635 PRK10635
bacterioferritin; Provisional
 1-153 6.90e-39

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 129.57  E-value: 6.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   1 MQGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPR-EFTPG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLgKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421772393  80 TTVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQ 153
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 13-143 1.26e-32

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: 112.76  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  13 DLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPREF------TPGTTVPEML 86
Cdd:pfam00210   6 EQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELlaieapPSFGSVLEVL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1421772393  87 RKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIER 143
Cdd:pfam00210  86 EAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDE-QEEHEWFLEALLEKLER 141
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
37-129 1.12e-05

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 43.02  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  37 FVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPREFTPGTTV-PE---------MLRKDLDTEYEVRAALQKGVQL 106
Cdd:NF041388   54 FRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVePEgedvydirtSLENDLEMYGDIIESVRDHIEL 133

                          90       100
                  ....*....|....*....|...
gi 1421772393 107 CESVRDYVSRDILLAQLRDTEED 129
Cdd:NF041388  134 AENLGDHATAELLREQLVELEED 156
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 6.21e-75

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: 220.50  E-value: 6.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   2 QGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPRE-FTPGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1421772393  81 TVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLrDTEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-153 7.20e-73

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 215.44  E-value: 7.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   3 GNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPR-EFTPGTT 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLgKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421772393  82 VPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQ 151
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-153 1.24e-41

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: 136.48  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   1 MQGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDM-RPREFTPG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421772393  80 TTVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDTEEdHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQ 153
PRK10635 PRK10635
bacterioferritin; Provisional
 1-153 6.90e-39

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 129.57  E-value: 6.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   1 MQGNPQVVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPR-EFTPG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLgKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421772393  80 TTVPEMLRKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIERVGLPNYLQSQ 153
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQ 153
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 13-143 1.26e-32

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: 112.76  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  13 DLLRGELAARDQYFIHSRIYEDQGFVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPREF------TPGTTVPEML 86
Cdd:pfam00210   6 EQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELlaieapPSFGSVLEVL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1421772393  87 RKDLDTEYEVRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQLGLIER 143
Cdd:pfam00210  86 EAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDE-QEEHEWFLEALLEKLER 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 3.09e-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: 60.20  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   9 DYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLnheMEEETQHADALLRRILFLGGLPDMRPR-------EFTPGTT 81
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEI---ADEERRHADALAERLRELGGTPPLPPAhllaayaLPKTSDD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1421772393  82 VPEMLRKDLDTEyevRAALQKGVQLCESVRDYVSRDILLAQLRDtEEDHAYWLEKQL 138
Cdd:cd00657    78 PAEALRAALEVE---ARAIAAYRELIEQADDPELRRLLERILAD-EQRHAAWFRKLL 130
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 46-130 1.14e-08

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: 50.99  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  46 HEMEEE-----TQHADALLRRILFLGGLPDMRPREFTPGTTVPE----------MLRKDLDTEYEVRAALQKGVQLCESV 110
Cdd:COG0783    48 HELFEElydelREAIDEIAERIRALGGVPPGTLAEFAKLSTIKEepegvvdareMVEALLEDYEALIKTLREAIELADEA 127

                          90       100
                  ....*....|....*....|
gi 1421772393 111 RDYVSRDILLAQLRDTEEDH 130
Cdd:COG0783   128 GDEGTADLLTDILRELEKRA 147
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 42-143 5.96e-06

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 43.74  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  42 ERLNHEMEEETQHADALLRRILFLGGLPDMRPREFT---------PG--TTVPEMLRKDLDTEyevRAALQKGVQLCESV 110
Cdd:COG2406    52 EELEDHAEEELNHAELLAERIYELGGTPPLDPEEWAelsgcgydlPEdpTDVRAILEQNLKAE---RCAIKVYNELCNMT 128

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1421772393 111 R--DYVSRDILLAQLRDtEEDHAYWLEKQLGLIER 143
Cdd:COG2406   129 KgkDPVTYDLALDILEE-EVEHEQDLEDLLGDLES 162
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
37-129 1.12e-05

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 43.02  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  37 FVKLYERLNHEMEEETQHADALLRRILFLGGLPDMRPREFTPGTTV-PE---------MLRKDLDTEYEVRAALQKGVQL 106
Cdd:NF041388   54 FRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVePEgedvydirtSLENDLEMYGDIIESVRDHIEL 133

                          90       100
                  ....*....|....*....|...
gi 1421772393 107 CESVRDYVSRDILLAQLRDTEED 129
Cdd:NF041388  134 AENLGDHATAELLREQLVELEED 156
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 46-129 1.18e-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: 39.84  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  46 HEMEEE-----TQHADALLRRILFLGGLPDMRPREFTPGTTVPE----------MLRKDLDTEYEVRAALQKGVQLCESV 110
Cdd:cd01043    33 HELFEElydelREAIDEIAERIRALGGKPLGTLKEYAELSTIKEepagvlsakeMVAELLEDYETLIEELREAIELADEA 112

                          90
                  ....*....|....*....
gi 1421772393 111 RDYVSRDILLAQLRDTEED 129
Cdd:cd01043   113 GDPATADLLTEIIRELEKQ 131
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
7-141 4.64e-04

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 38.17  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393   7 VVDYFKDLLRGELAARDQYFIHSRIYEDQGFVKLYERLnheMEEETQHADALLRRILFLGGLPDMRPREFTPGTTVPEM- 85
Cdd:COG1633     2 LLEILKEAIAMEEEAIEFYLELAEKAKDPELKKLFEEL---AEEEKKHAELLEKLYEKLGGKPVAPPEEESQPGLAELMd 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421772393  86 -LRKDLDTEYEVRAALQKG-------VQLCESVRDYVSRDIlLAQLRDTEEDHAYWLEKQLGLI 141
Cdd:COG1633    79 kLDGSVSDAEALELAIATEkdaiefyRELAAKVGDPEIKKL-FEELAADEKEHAALLEGLYDRL 141
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 49-135 2.81e-03

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: 36.11  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421772393  49 EEETQHADALLRRILFLGGLPDMRPREFTP------------GTTVPEMLRKDLDTEyevRAALQKGVQLCESV--RDYV 114
Cdd:cd01052    49 EEELNHAELLAERIYELGGTPPRDPKDWYEisgckcgylppdPPDVKGILKVNLKAE---RCAIKVYKELCDMThgKDPV 125

                          90       100
                  ....*....|....*....|.
gi 1421772393 115 SRDILLAQLRDtEEDHAYWLE 135
Cdd:cd01052   126 TYDLALAILNE-EIEHEEDLE 145
 
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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