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Conserved domains on  [gi|50539816|ref|NP_001002378|]
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ferritin, heavy polypeptide-like 27 [Danio rerio]

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 ...
 10-170 3.22e-93

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: 267.87  E-value: 3.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  10 DRDCEALINKMINLELYAGYTYTSMAFYFDRDDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERDE 89
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  90 WDNGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLESHYLNEQVEAIKKLGDHITNLSKMDAGNNRMAEYLFDK 169
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                .
gi 50539816 170 H 170
Cdd:cd01056 161 Y 161
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 10-170 3.22e-93

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: 267.87  E-value: 3.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  10 DRDCEALINKMINLELYAGYTYTSMAFYFDRDDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERDE 89
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  90 WDNGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLESHYLNEQVEAIKKLGDHITNLSKMDAGNNRMAEYLFDK 169
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                .
gi 50539816 170 H 170
Cdd:cd01056 161 Y 161
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 14-154 9.38e-36

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: 121.24  E-value: 9.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816    14 EALINKMINLELYAGYTYTSMAFYFDrdDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERD---EW 90
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50539816    91 DNGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLEsHYLNEQVEAIKKLGDHITNLSK 154
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
14-170 3.92e-33

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 115.23  E-value: 3.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  14 EALINKMINLELYAGYTYTSMAFYFDRDDvaLPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERdEWDNG 93
Cdd:COG1528   7 EKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EFESL 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50539816  94 LTAMQCALQLEKNVNQALLDLHKVASQKGDpHLC-DFLEShYLNEQVEAIKKLGDHITNLsKMdAGNNRMAEYLFDKH 170
Cdd:COG1528  84 LEVFEAALEHEQKVTKSINELVDLAREEKD-YATeNFLQW-FVKEQVEEEALARTILDKL-KL-AGDDGSGLFMLDKE 157
PRK10304 PRK10304
non-heme ferritin;
17-174 1.42e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 40.41  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816   17 INKMINLELYAGYTYTSMAFYFDRDdvALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPeRDEWDNGLTA 96
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSLDEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816   97 MQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLEsHYLNEQVEAIKKLGDHITNLSKmdAGNNRMAEYLFDKH--TLDS 174
Cdd:PRK10304  87 FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQ-WYVSEQHEEEKLFKSIIDKLSL--AGKSGEGLYFIDKElsTLDT 163
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 10-170 3.22e-93

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: 267.87  E-value: 3.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  10 DRDCEALINKMINLELYAGYTYTSMAFYFDRDDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERDE 89
Cdd:cd01056   1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  90 WDNGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLESHYLNEQVEAIKKLGDHITNLSKMDAGNNRMAEYLFDK 169
Cdd:cd01056  81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                .
gi 50539816 170 H 170
Cdd:cd01056 161 Y 161
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 12-169 8.14e-78

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: 228.69  E-value: 8.14e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  12 DCEALINKMINLELYAGYTYTSMAFYFDRDDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERDEWD 91
Cdd:cd00904   3 KVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPSDEWG 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50539816  92 NGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLESHYLNEQVEAIKKLGDHITNLSKMDAGNNRMAEYLFDK 169
Cdd:cd00904  83 GTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLNGQQAGSGEYLFDR 160
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 14-154 9.38e-36

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: 121.24  E-value: 9.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816    14 EALINKMINLELYAGYTYTSMAFYFDrdDVALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERD---EW 90
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50539816    91 DNGLTAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLEsHYLNEQVEAIKKLGDHITNLSK 154
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 14-170 1.87e-33

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: 116.05  E-value: 1.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  14 EALINKMINLELYAGYTYTSMAFYFDRDDvaLPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERdEWDNG 93
Cdd:cd01055   5 EKALNEQINLELYSSYLYLAMAAWFDSKG--LDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPS-EFESL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50539816  94 LTAMQCALQLEKNVNQALLDLHKVASQKGDpHLC-DFLEShYLNEQVEAIKKLGDHITNLsKMdAGNNRMAEYLFDKH 170
Cdd:cd01055  82 LEVFEAALEHEQKVTESINNLVDLALEEKD-YATfNFLQW-FVKEQVEEEALARDILDKL-KL-AGDDGGGLYMLDKE 155
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
14-170 3.92e-33

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 115.23  E-value: 3.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  14 EALINKMINLELYAGYTYTSMAFYFDRDDvaLPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPERdEWDNG 93
Cdd:COG1528   7 EKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EFESL 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50539816  94 LTAMQCALQLEKNVNQALLDLHKVASQKGDpHLC-DFLEShYLNEQVEAIKKLGDHITNLsKMdAGNNRMAEYLFDKH 170
Cdd:COG1528  84 LEVFEAALEHEQKVTKSINELVDLAREEKD-YATeNFLQW-FVKEQVEEEALARTILDKL-KL-AGDDGSGLFMLDKE 157
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
15-146 2.10e-06

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 45.18  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  15 ALINKMINLELYAGYTYTSMAFYFDrdDVALPGFAKFFKKNSEEEREHAEKFMEfqnkR----GGRIVLQDIKK------ 84
Cdd:COG2193   7 ELLNKALANELTAINQYFLHARMLK--NWGLEKLAEKFYEESIEEMKHADKLIE----RilflGGLPNLQDLGKlriged 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50539816  85 -PErdewdngltAMQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLES---------HYLNEQVEAIKKLG 146
Cdd:COG2193  81 vEE---------MLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEiledeeehiDWLETQLELIEKIG 143
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 15-132 1.09e-05

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: 42.87  E-value: 1.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  15 ALINKMINLELYAGYTYTSMAFYFDRDDVAlpgfaKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKP----ERDEW 90
Cdd:cd00657   1 RLLNDALAGEYAAIIAYGQLAARAPDPDLK-----DELLEIADEERRHADALAERLRELGGTPPLPPAHLLaayaLPKTS 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 50539816  91 DNGLTAMQCALQLEKNVNQALLDLHKVAsqkGDPHLCDFLES 132
Cdd:cd00657  76 DDPAEALRAALEVEARAIAAYRELIEQA---DDPELRRLLER 114
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 49-148 1.83e-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: 42.53  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816  49 AKFFKKNSEEEREHAEKFMEfqnkR----GGRIVLQDIKKPERDEwdnGLTAM-QCALQLEKNVNQALLDLHKVASQKGD 123
Cdd:cd00907  40 AERFRKESIEEMKHADKLIE----RilflEGLPNLQRLGKLRIGE---DVPEMlENDLALEYEAIAALNEAIALCEEVGD 112

                        90       100       110
                ....*....|....*....|....*....|....
gi 50539816 124 PHLCDFLES---------HYLNEQVEAIKKLGDH 148
Cdd:cd00907 113 YVSRDLLEEiledeeehiDWLETQLDLIDKMGLQ 146
PRK10304 PRK10304
non-heme ferritin;
17-174 1.42e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 40.41  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816   17 INKMINLELYAGYTYTSMAFYFDRDdvALPGFAKFFKKNSEEEREHAEKFMEFQNKRGGRIVLQDIKKPeRDEWDNGLTA 96
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSLDEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539816   97 MQCALQLEKNVNQALLDLHKVASQKGDPHLCDFLEsHYLNEQVEAIKKLGDHITNLSKmdAGNNRMAEYLFDKH--TLDS 174
Cdd:PRK10304  87 FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQ-WYVSEQHEEEKLFKSIIDKLSL--AGKSGEGLYFIDKElsTLDT 163
 
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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