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Conserved domains on  [gi|1965291793|ref|XP_039038860|]
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ferritin-3, chloroplastic-like [Hibiscus syriacus]

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 ...
 134-294 1.01e-80

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: 241.29  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPfsef 213
Cdd:cd01056     1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 YHVEKGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESEYLAEQVEAIKKISEYVAQLRRVGK---GHGVW 290
Cdd:cd01056    77 EKDEWGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEY 156


                  ....
gi 1965291793 291 HFDQ 294
Cdd:cd01056   157 LFDK 160
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 134-294 1.01e-80

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: 241.29  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPfsef 213
Cdd:cd01056     1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 YHVEKGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESEYLAEQVEAIKKISEYVAQLRRVGK---GHGVW 290
Cdd:cd01056    77 EKDEWGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEY 156


                  ....
gi 1965291793 291 HFDQ 294
Cdd:cd01056   157 LFDK 160
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 138-282 9.97e-31

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 112.38  E-value: 9.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 138 EAAINEQINVEYNVSYVYHAMFAYFDrdNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSIlmpfsEFYHVE 217
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRV-----ELLAIE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1965291793 218 K----GDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVEsEYLAEQVEAIKKISEYVAQLRR 282
Cdd:pfam00210  74 AppsfGSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
134-296 4.93e-29

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 108.68  E-value: 4.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNvaLRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEF 213
Cdd:COG1528     3 SEKMEKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 yhvekGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVEsEYLAEQVEAIKKISEYVAQLRRVGK-GHGVWHF 292
Cdd:COG1528    81 -----ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQ-WFVKEQVEEEALARTILDKLKLAGDdGSGLFML 154


                  ....
gi 1965291793 293 DQML 296
Cdd:COG1528   155 DKEL 158
PRK10304 PRK10304
non-heme ferritin;
141-296 1.86e-10

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 58.52  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 141 INEQINVEYNVSYVYHAMFAYFDRDnvALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEFYHVekgD 220
Cdd:PRK10304   10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEYSSL---D 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1965291793 221 ALYamELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESeYLAEQVEAIKKISEYVAQLRRVGK-GHGVWHFDQML 296
Cdd:PRK10304   85 ELF--QETYKHEQLITQKINELAHAAMTNQDYPTFNFLQW-YVSEQHEEEKLFKSIIDKLSLAGKsGEGLYFIDKEL 158
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 134-294 1.01e-80

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: 241.29  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPfsef 213
Cdd:cd01056     1 HEECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 YHVEKGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESEYLAEQVEAIKKISEYVAQLRRVGK---GHGVW 290
Cdd:cd01056    77 EKDEWGSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKpqsGLGEY 156


                  ....
gi 1965291793 291 HFDQ 294
Cdd:cd01056   157 LFDK 160
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 134-294 4.18e-47

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: 155.50  E-value: 4.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEf 213
Cdd:cd00904     1 SEKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPSD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 yhvEKGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESEYLAEQVEAIKKISEYVAQLRRVG---KGHGVW 290
Cdd:cd00904    80 ---EWGGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLNgqqAGSGEY 156


                  ....
gi 1965291793 291 HFDQ 294
Cdd:cd00904   157 LFDR 160
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 134-296 4.66e-31

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: 113.74  E-value: 4.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNvaLRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEF 213
Cdd:cd01055     1 SEKLEKALNEQINLELYSSYLYLAMAAWFDSKG--LDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 yhvekGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVEsEYLAEQVEAIKKISEYVAQLRRVGK-GHGVWHF 292
Cdd:cd01055    79 -----ESLLEVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQ-WFVKEQVEEEALARDILDKLKLAGDdGGGLYML 152


                  ....
gi 1965291793 293 DQML 296
Cdd:cd01055   153 DKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 138-282 9.97e-31

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 112.38  E-value: 9.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 138 EAAINEQINVEYNVSYVYHAMFAYFDrdNVALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSIlmpfsEFYHVE 217
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVK--GPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRV-----ELLAIE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1965291793 218 K----GDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVEsEYLAEQVEAIKKISEYVAQLRR 282
Cdd:pfam00210  74 AppsfGSVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
134-296 4.93e-29

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 108.68  E-value: 4.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 134 SDECEAAINEQINVEYNVSYVYHAMFAYFDRDNvaLRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEF 213
Cdd:COG1528     3 SEKMEKALNEQINLEFYSSYLYLAMAAWCDEKG--LPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 214 yhvekGDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVEsEYLAEQVEAIKKISEYVAQLRRVGK-GHGVWHF 292
Cdd:COG1528    81 -----ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQ-WFVKEQVEEEALARTILDKLKLAGDdGSGLFML 154


                  ....
gi 1965291793 293 DQML 296
Cdd:COG1528   155 DKEL 158
PRK10304 PRK10304
non-heme ferritin;
141-296 1.86e-10

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 58.52  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 141 INEQINVEYNVSYVYHAMFAYFDRDnvALRGLAKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEFYHVekgD 220
Cdd:PRK10304   10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEYSSL---D 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1965291793 221 ALYamELALSLEKLTNEKLLNLHGVAERNHDVQLTHFVESeYLAEQVEAIKKISEYVAQLRRVGK-GHGVWHFDQML 296
Cdd:PRK10304   85 ELF--QETYKHEQLITQKINELAHAAMTNQDYPTFNFLQW-YVSEQHEEEKLFKSIIDKLSLAGKsGEGLYFIDKEL 158
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 139-256 3.78e-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: 42.48  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965291793 139 AAINEQINVEYNVSYVYHAMFAYFDRDNVAlrglaKFFKESSLEEREHAEKLMEYQNKRGGKVKLQSILMPFSEFYHVEK 218
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLK-----DELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTS 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1965291793 219 GDALYAMELALSLEKLTNEKLLNLHGVAERNHDVQLTH 256
Cdd:cd00657    76 DDPAEALRAALEVEARAIAAYRELIEQADDPELRRLLE 113
 
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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