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Conserved domains on  [gi|1806247385|dbj|BBX37308|]
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bacterioferritin [Mycolicibacterium mageritense]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ferritin_like super family cl00264
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 1-157 4.41e-77

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).


The actual alignment was detected with superfamily member TIGR00754:

Pssm-ID: 469698  Cd Length: 157  Bit Score: 226.23  E-value: 4.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   1 MQGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806247385  81 QTLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQCVSRP 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
 
Name Accession Description Interval E-value
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 4.41e-77

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: 226.23  E-value: 4.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   1 MQGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806247385  81 QTLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQCVSRP 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-152 4.29e-76

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: 223.58  E-value: 4.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   2 QGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVGQ 81
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806247385  82 TLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQ 152
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQS 151
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-152 1.12e-69

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 207.35  E-value: 1.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   3 GDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVGQT 82
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385  83 LREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQ 152
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQS 150
PRK10635 PRK10635
bacterioferritin; Provisional
 1-149 2.36e-42

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 138.04  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   1 MQGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1806247385  81 QTLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLY 149
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNY 149
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 9.38e-35

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: 9.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   8 LKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRL-----FSLRVGQT 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVellaiEAPPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806247385  83 LREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDK 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
 
Name Accession Description Interval E-value
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 4.41e-77

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: 226.23  E-value: 4.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   1 MQGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806247385  81 QTLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQCVSRP 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-152 4.29e-76

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: 223.58  E-value: 4.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   2 QGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVGQ 81
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806247385  82 TLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQ 152
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQS 151
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-152 1.12e-69

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 207.35  E-value: 1.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   3 GDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVGQT 82
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385  83 LREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLYAAQ 152
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQS 150
PRK10635 PRK10635
bacterioferritin; Provisional
 1-149 2.36e-42

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 138.04  E-value: 2.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   1 MQGDADVLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFSLRVG 80
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1806247385  81 QTLREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDKLGEQLY 149
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNY 149
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 9.38e-35

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: 9.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   8 LKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRL-----FSLRVGQT 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVellaiEAPPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806247385  83 LREQFEADLAIEYEVVARLKPGIIMCREKQDAVTANLFETILGDEEGHIDYLETQLELMDK 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 4.71e-10

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: 54.42  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   9 KLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRsesFEEMRHAEAITDRILLLDGLPNYQRLFSLRVGQ------T 82
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIA---DEERRHADALAERLRELGGTPPLPPAHLLAAYAlpktsdD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806247385  83 LREQFEADLAIEYEVVARLKpgiIMCREKQDAVTANLFETILGDEEGHIDYLETQL 138
Cdd:cd00657    78 PAEALRAALEVEARAIAAYR---ELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 16-138 1.16e-08

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: 51.12  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385  16 TSELTAINQYFLHSKMQDNwGFTELAAHTRSESFEEMRHAEAITDRILLLDGLPNYQRLFS----------LRVGQTLRE 85
Cdd:cd07908    26 NSELTAISQYIYQHLISEE-KYPEIAETFLGIAIVEMHHLEILGQLIVLLGGDPRYRSSSSdkftywtgkyVNYGESIKE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806247385  86 QFEADLAIEYEVVARLKPGIIMCreKQDAVTANLfETILGDEEGHIDYLETQL 138
Cdd:cd07908   105 MLKLDIASEKAAIAKYKRQAETI--KDPYIRALL-NRIILDEKLHIKILEELL 154
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 7-139 3.22e-04

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 39.11  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   7 VLKLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRSESFEEMRHAEAITDRILLLDGLP--NYQRLFSL-RVGQ-- 81
Cdd:COG2406    17 LIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPplDPEEWAELsGCGYdl 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806247385  82 -----TLREQFEADLAIEYEVVARLKPGIIMCREKqDAVTANLFETILGDEEGHIDYLETQLE 139
Cdd:COG2406    97 pedptDVRAILEQNLKAERCAIKVYNELCNMTKGK-DPVTYDLALDILEEEVEHEQDLEDLLG 158
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
6-141 3.85e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 35.85  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806247385   6 DVLKLLNEQLTSELTAINQY-FLHSKMQDNWG---FTELAAhtrsesfEEMRHAEAITDRILLLDG----------LPNY 71
Cdd:COG1633     1 SLLEILKEAIAMEEEAIEFYlELAEKAKDPELkklFEELAE-------EEKKHAELLEKLYEKLGGkpvappeeesQPGL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806247385  72 QRLF-SLRVGQTLREQFEADLAIEYEVVARLKpgiIMCREKQDAVTANLFETILGDEEGHIDYLETQLELM 141
Cdd:COG1633    74 AELMdKLDGSVSDAEALELAIATEKDAIEFYR---ELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 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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