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Conserved domains on  [gi|498948392|ref|XP_004543325|]
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ferritin, heavy subunit [Maylandia zebra]

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 4.94e-96

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: 274.81  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  10 HQDCEAAVNRQINLELYASYVYLSMSYYFDRDDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRDE 89
Cdd:cd01056    1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  90 WGSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIENHYLDEQVKSIKELADWVTNLRRMGAPQNGMAEYLFDK 169
Cdd:cd01056   81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                 .
gi 498948392 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 4.94e-96

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: 274.81  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  10 HQDCEAAVNRQINLELYASYVYLSMSYYFDRDDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRDE 89
Cdd:cd01056    1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  90 WGSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIENHYLDEQVKSIKELADWVTNLRRMGAPQNGMAEYLFDK 169
Cdd:cd01056   81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                 .
gi 498948392 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 9.27e-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: 126.63  E-value: 9.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392   14 EAAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRD---EW 90
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498948392   91 GSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRR 154
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
14-170 2.89e-35

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 120.62  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  14 EAAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRdEWGSG 93
Cdd:COG1528    7 EKALNEQINLEFYSSYLYLAMAAWCD--EKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EFESL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498948392  94 VEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIeNHYLDEQVKSIKELADWVTNLRRMGapQNGMAEYLFDKH 170
Cdd:COG1528   84 LEVFEAALEHEQKVTKSINELVDLAREEKDYATENFL-QWFVKEQVEEEALARTILDKLKLAG--DDGSGLFMLDKE 157
PRK10304 PRK10304
non-heme ferritin;
17-169 2.37e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 39.64  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  17 VNRQINLELYASYVYLSMSYYFdrddqALHNF---AKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPdRDEWGSG 93
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWC-----SYHTFegaAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498948392  94 VEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRRMGAPQNGMaeYLFDK 169
Cdd:PRK10304  84 DELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQ-WYVSEQHEEEKLFKSIIDKLSLAGKSGEGL--YFIDK 156
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 10-170 4.94e-96

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: 274.81  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  10 HQDCEAAVNRQINLELYASYVYLSMSYYFDRDDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRDE 89
Cdd:cd01056    1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  90 WGSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIENHYLDEQVKSIKELADWVTNLRRMGAPQNGMAEYLFDK 169
Cdd:cd01056   81 WGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDK 160


                 .
gi 498948392 170 H 170
Cdd:cd01056  161 Y 161
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 10-169 2.22e-77

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: 227.91  E-value: 2.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  10 HQDCEAAVNRQINLELYASYVYLSMSYYFDRDDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRDE 89
Cdd:cd00904    1 SEKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPSDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  90 WGSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIENHYLDEQVKSIKELADWVTNLRRMGAPQNGMAEYLFDK 169
Cdd:cd00904   81 WGGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLNGQQAGSGEYLFDR 160
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 14-154 9.27e-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: 126.63  E-value: 9.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392   14 EAAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRD---EW 90
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEappSF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498948392   91 GSGVEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRR 154
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
14-170 2.89e-35

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 120.62  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  14 EAAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPDRdEWGSG 93
Cdd:COG1528    7 EKALNEQINLEFYSSYLYLAMAAWCD--EKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPN-EFESL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498948392  94 VEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIeNHYLDEQVKSIKELADWVTNLRRMGapQNGMAEYLFDKH 170
Cdd:COG1528   84 LEVFEAALEHEQKVTKSINELVDLAREEKDYATENFL-QWFVKEQVEEEALARTILDKLKLAG--DDGSGLFMLDKE 157
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 14-170 1.41e-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: 116.43  E-value: 1.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  14 EAAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPdRDEWGSG 93
Cdd:cd01055    5 EKALNEQINLELYSSYLYLAMAAWFD--SKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAP-PSEFESL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498948392  94 VEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIeNHYLDEQVKSIKELADWVTNLRRMGAPQNGMaeYLFDKH 170
Cdd:cd01055   82 LEVFEAALEHEQKVTESINNLVDLALEEKDYATFNFL-QWFVKEQVEEEALARDILDKLKLAGDDGGGL--YMLDKE 155
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 15-160 5.05e-07

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: 46.77  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  15 AAVNRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKlqnqrggRI-FLQ---DVKKPDRDEW 90
Cdd:cd00907    8 EALNKALTGELTAINQYFLHARMLE--DWGLEKLAERFRKESIEEMKHADKLIE-------RIlFLEglpNLQRLGKLRI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498948392  91 GSGV-EALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRRMGaPQN 160
Cdd:cd00907   79 GEDVpEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLDLIDKMG-LQN 147
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
18-158 5.29e-07

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 46.73  E-value: 5.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  18 NRQINLELYASYVYLSMSYYFDrdDQALHNFAKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPdrdEWGSGV-EA 96
Cdd:COG2193   10 NKALANELTAINQYFLHARMLK--NWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKL---RIGEDVeEM 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498948392  97 LECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRRMGAP 158
Cdd:COG2193   85 LECDLALELEAIALYREAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLELIEKIGLQ 145
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 15-139 4.17e-06

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: 44.02  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  15 AAVNRQINLELYASYVYLSMSYYFDRDDqalhnFAKFFHHQSHEEREHAEKLMKLQNQRGGRI-FLQDVKKPDRDEWGSG 93
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPD-----LKDELLEIADEERRHADALAERLRELGGTPpLPPAHLLAAYALPKTS 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 498948392  94 ---VEALECALQLEKSVNQSLLDLHKLCSehnDPHMCDFIENHYLDEQV 139
Cdd:cd00657   76 ddpAEALRAALEVEARAIAAYRELIEQAD---DPELRRLLERILADEQR 121
PRK10304 PRK10304
non-heme ferritin;
17-169 2.37e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 39.64  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498948392  17 VNRQINLELYASYVYLSMSYYFdrddqALHNF---AKFFHHQSHEEREHAEKLMKLQNQRGGRIFLQDVKKPdRDEWGSG 93
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWC-----SYHTFegaAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESP-FAEYSSL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498948392  94 VEALECALQLEKSVNQSLLDLHKLCSEHNDPHMCDFIEnHYLDEQVKSIKELADWVTNLRRMGAPQNGMaeYLFDK 169
Cdd:PRK10304  84 DELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQ-WYVSEQHEEEKLFKSIIDKLSLAGKSGEGL--YFIDK 156
 
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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