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Conserved domains on  [gi|1829097571|pdb|6LP5|F]
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Chain F, Ferritin

Protein Classification

ferritin( domain architecture ID 10099405)

ferritin is the primary iron storage protein of most living organisms and belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 11-167 2.80e-94

eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues.


:

Pssm-ID: 153114  Cd Length: 161  Bit Score: 270.18  E-value: 2.80e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       11 HQDSEAGINKQINMELYASYVYQSMSFYFDRDDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRDE 90
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       91 WGSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGEYLEEQVEAIKDLSDRITNLNRVGK---GLGEWHYDQ 167
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEYLFDK 160
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 11-167 2.80e-94

eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues.


Pssm-ID: 153114  Cd Length: 161  Bit Score: 270.18  E-value: 2.80e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       11 HQDSEAGINKQINMELYASYVYQSMSFYFDRDDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRDE 90
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       91 WGSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGEYLEEQVEAIKDLSDRITNLNRVGK---GLGEWHYDQ 167
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEYLFDK 160
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 15-155 1.74e-38

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: 128.17  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F         15 EAGINKQINMELYASYVYQSMSFYFDrdDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRD---EW 91
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
6LP5_F         92 GSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEgEYLEEQVEAIKDLSDRITNLNR 155
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
12-169 3.76e-38

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 127.94  E-value: 3.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       12 QDSEAGINKQINMELYASYVYQSMSFYFDRDDvaLKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRdEW 91
Cdd:COG1528   4 EKMEKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6LP5_F       92 GSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGeYLEEQVEAIKDLSDRITNLNRVGK-GLGEWHYDQKL 169
Cdd:COG1528  81 ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQW-FVKEQVEEEALARTILDKLKLAGDdGSGLFMLDKEL 158
PRK10304 PRK10304
non-heme ferritin;
18-169 1.04e-11

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 59.67  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F        18 INKQINMELYASYVYQSMSFYFDRDdvALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPdRDEWGSGLDA 97
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSLDEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6LP5_F        98 MKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGeYLEEQVEAIKDLSDRITNLNRVGK-GLGEWHYDQKL 169
Cdd:PRK10304  87 FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQW-YVSEQHEEEKLFKSIIDKLSLAGKsGEGLYFIDKEL 158
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 11-167 2.80e-94

eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues.


Pssm-ID: 153114  Cd Length: 161  Bit Score: 270.18  E-value: 2.80e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       11 HQDSEAGINKQINMELYASYVYQSMSFYFDRDDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRDE 90
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       91 WGSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGEYLEEQVEAIKDLSDRITNLNRVGK---GLGEWHYDQ 167
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEYLFDK 160
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 11-167 6.03e-66

Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living organisms and members of a broad superfamily of ferritin-like diiron-carboxylate proteins. The iron-free (apoferritin) ferritin molecule is a protein shell composed of 24 protein chains arranged in 432 symmetry. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the dinuclear ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite; the protein shell can hold up to 4500 iron atoms. In vertebrates, two types of chains (subunits) have been characterized, H or M (fast) and L (slow), which differ in rates of iron uptake and mineralization. Bacterial non-heme ferritins are composed only of H chains. Fe(II) oxidation in the H/M subunits take place initially at the ferroxidase center, a carboxylate-bridged diiron center, located within the subunit four-helix bundle. In a complementary role, negatively charged residues on the protein shell inner surface of the L subunits promote ferrihydrite nucleation. Most plant ferritins combine both oxidase and nucleation functions in one chain: they have four interior glutamate residues as well as seven ferroxidase center residues.


Pssm-ID: 153098  Cd Length: 160  Bit Score: 198.64  E-value: 6.03e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       11 HQDSEAGINKQINMELYASYVYQSMSFYFDRDDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRDE 90
Cdd:cd00904   1 SEKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPSDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       91 WGSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGEYLEEQVEAIKDLSDRITNLNRVG---KGLGEWHYDQ 167
Cdd:cd00904  81 WGGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLNgqqAGSGEYLFDR 160
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 18-169 6.13e-40

nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite.


Pssm-ID: 153113  Cd Length: 156  Bit Score: 132.23  E-value: 6.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       18 INKQINMELYASYVYQSMSFYFDRDDvaLKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPdRDEWGSGLDA 97
Cdd:cd01055   8 LNEQINLELYSSYLYLAMAAWFDSKG--LDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAP-PSEFESLLEV 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6LP5_F       98 MKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEgEYLEEQVEA---IKDLSDRITNLNRVGKGLgeWHYDQKL 169
Cdd:cd01055  85 FEAALEHEQKVTESINNLVDLALEEKDYATFNFLQ-WFVKEQVEEealARDILDKLKLAGDDGGGL--YMLDKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 15-155 1.74e-38

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: 128.17  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F         15 EAGINKQINMELYASYVYQSMSFYFDrdDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRD---EW 91
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
6LP5_F         92 GSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEgEYLEEQVEAIKDLSDRITNLNR 155
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
12-169 3.76e-38

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 127.94  E-value: 3.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       12 QDSEAGINKQINMELYASYVYQSMSFYFDRDDvaLKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDRdEW 91
Cdd:COG1528   4 EKMEKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6LP5_F       92 GSGLDAMKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGeYLEEQVEAIKDLSDRITNLNRVGK-GLGEWHYDQKL 169
Cdd:COG1528  81 ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQW-FVKEQVEEEALARTILDKLKLAGDdGSGLFMLDKEL 158
PRK10304 PRK10304
non-heme ferritin;
18-169 1.04e-11

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 59.67  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F        18 INKQINMELYASYVYQSMSFYFDRDdvALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPdRDEWGSGLDA 97
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSLDEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6LP5_F        98 MKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGeYLEEQVEAIKDLSDRITNLNRVGK-GLGEWHYDQKL 169
Cdd:PRK10304  87 FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQW-YVSEQHEEEKLFKSIIDKLSLAGKsGEGLYFIDKEL 158
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 18-142 9.28e-08

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: 48.26  E-value: 9.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       18 INKQINMELYASYVYQSMSFYFDRDDVAlkgfaKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDR----DEWGS 93
Cdd:cd00657   3 LNDALAGEYAAIIAYGQLAARAPDPDLK-----DELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAyalpKTSDD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
6LP5_F       94 GLDAMKAALNLEKSVNQSLLELHKVADSHGDAqmcDFLEGEYLEEQVEA 142
Cdd:cd00657  78 PAEALRAALEVEARAIAAYRELIEQADDPELR---RLLERILADEQRHA 123
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 19-146 1.26e-05

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: 42.92  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       19 NKQINMELYAS--YVYQSMSFyfdrDDVALKGFAKFFKESSDEEREHAEKLMkyqnKR----GGRIVLQPISKPdrdEWG 92
Cdd:cd00907  11 NKALTGELTAInqYFLHARML----EDWGLEKLAERFRKESIEEMKHADKLI----ERilflEGLPNLQRLGKL---RIG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
6LP5_F       93 SGLDAM-KAALNLEKSVNQSLLELHKVADSHGDAQMCDFLE---------GEYLEEQVEAIKDL 146
Cdd:cd00907  80 EDVPEMlENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEeiledeeehIDWLETQLDLIDKM 143
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
19-157 1.85e-05

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 42.49  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F       19 NKQINMELYASYVYQSMSFYFDrdDVALKGFAKFFKESSDEEREHAEKLMkyqnKR----GGRIVLQPISKPdrdEWGSG 94
Cdd:COG2193  10 NKALANELTAINQYFLHARMLK--NWGLEKLAEKFYEESIEEMKHADKLI----ERilflGGLPNLQDLGKL---RIGED 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
6LP5_F       95 LDAM-KAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEgEYLEEQVEAIKDLSDRITNLNRVG 157
Cdd:COG2193  81 VEEMlECDLALELEAIALYREAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLELIEKIG 143
PRK15022 PRK15022
non-heme ferritin-like protein;
18-170 4.73e-03

non-heme ferritin-like protein;


Pssm-ID: 184983  Cd Length: 167  Bit Score: 36.01  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LP5_F        18 INKQINMELYASYVYQSMSFYFdrDDVALKGFAKFFKESSDEEREHAEKLMKYQNKRGGRIVLQPISKPDrDEWGSGLDA 97
Cdd:PRK15022  10 LNSQMNLEFYASNLYLHLSEWC--SEQSLNGTATFLRAQAQSNVTQMMRMFNFMKSAGATPIVKAIDVPG-EKLNSLEEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6LP5_F        98 MKAALNLEKSVNQSLLELHKVADSHGDAQMCDFLEGEYLEEQVEAI--KDLSDRITNLNRVGKGLGEwhYDQKLL 170
Cdd:PRK15022  87 FQKTLEEYEQRSSTLAQLADEAKALNDDSTLNFLRDLEKEQQHDGLllQTILDEVRSAKLAGLCPVQ--TDQHLL 159
 
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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