NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2068667744|ref|XP_042231306|]
View 

ferritin subunit-like [Homarus americanus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 39-205 5.17e-32

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 cd01056:

Pssm-ID: 469698  Cd Length: 161  Bit Score: 113.79  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  39 CAVAVKGQIQHELNAAFGYMYMGAYFAQYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTS 118
Cdd:cd01056     4 CEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744 119 FVgktrpykAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNPILDEQHNGVRKLQGAVktyADLH--LNQENDe 194
Cdd:cd01056    84 GL-------EALELALDLEKLVNQSLLDLHKLASEhnDPHLADFLESEFLEEQVESIKKLAGYI---TNLKrvGKPQSG- 152

                         170
                  ....*....|.
gi 2068667744 195 aaaaLAEYIFD 205
Cdd:cd01056   153 ----LGEYLFD 159
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 39-205 5.17e-32

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: 113.79  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  39 CAVAVKGQIQHELNAAFGYMYMGAYFAQYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTS 118
Cdd:cd01056     4 CEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744 119 FVgktrpykAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNPILDEQHNGVRKLQGAVktyADLH--LNQENDe 194
Cdd:cd01056    84 GL-------EALELALDLEKLVNQSLLDLHKLASEhnDPHLADFLESEFLEEQVESIKKLAGYI---TNLKrvGKPQSG- 152

                         170
                  ....*....|.
gi 2068667744 195 aaaaLAEYIFD 205
Cdd:cd01056   153 ----LGEYLFD 159
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
46-170 3.84e-17

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 75.17  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  46 QIQHELNAAFGYMYMGAYFAQyaVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNI-----PNYTFNNnqlntsfv 120
Cdd:COG1528    13 QINLEFYSSYLYLAMAAWCDE--KGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELpaidaPPNEFES-------- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2068667744 121 gktrpYKAALEQALNMEIEVTNLIYNVVKECGE--DYhGADVFTNPILDEQH 170
Cdd:COG1528    83 -----LLEVFEAALEHEQKVTKSINELVDLAREekDY-ATENFLQWFVKEQV 128
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 46-177 4.98e-15

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: 68.85  E-value: 4.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  46 QIQHELNAAFGYMYMGAYFaqYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTSFvGKTRp 125
Cdd:pfam00210   7 QLADELTASYQYLQMHWYV--KGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSF-GSVL- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2068667744 126 ykAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNpILDEQHNGVRKLQ 177
Cdd:pfam00210  83 --EVLEAALEHEKKVTKSLRELIELAEEegDYATADFLQW-FLDEQEEHEWFLE 133
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 39-205 5.17e-32

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: 113.79  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  39 CAVAVKGQIQHELNAAFGYMYMGAYFAQYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTS 118
Cdd:cd01056     4 CEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744 119 FVgktrpykAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNPILDEQHNGVRKLQGAVktyADLH--LNQENDe 194
Cdd:cd01056    84 GL-------EALELALDLEKLVNQSLLDLHKLASEhnDPHLADFLESEFLEEQVESIKKLAGYI---TNLKrvGKPQSG- 152

                         170
                  ....*....|.
gi 2068667744 195 aaaaLAEYIFD 205
Cdd:cd01056   153 ----LGEYLFD 159
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 46-170 4.71e-18

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: 77.53  E-value: 4.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  46 QIQHELNAAFGYMYMGAYFAQyaVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNI-----PNYTFNNnqlntsfv 120
Cdd:cd01055    11 QINLELYSSYLYLAMAAWFDS--KGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELpaieaPPSEFES-------- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068667744 121 gktrpYKAALEQALNMEIEVTNLIYNVVKEC-GEDYHGADVFTNPILDEQH 170
Cdd:cd01055    81 -----LLEVFEAALEHEQKVTESINNLVDLAlEEKDYATFNFLQWFVKEQV 126
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
46-170 3.84e-17

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 75.17  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  46 QIQHELNAAFGYMYMGAYFAQyaVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNI-----PNYTFNNnqlntsfv 120
Cdd:COG1528    13 QINLEFYSSYLYLAMAAWCDE--KGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELpaidaPPNEFES-------- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2068667744 121 gktrpYKAALEQALNMEIEVTNLIYNVVKECGE--DYhGADVFTNPILDEQH 170
Cdd:COG1528    83 -----LLEVFEAALEHEQKVTKSINELVDLAREekDY-ATENFLQWFVKEQV 128
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 46-177 4.98e-15

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: 68.85  E-value: 4.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  46 QIQHELNAAFGYMYMGAYFaqYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTSFvGKTRp 125
Cdd:pfam00210   7 QLADELTASYQYLQMHWYV--KGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSF-GSVL- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2068667744 126 ykAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNpILDEQHNGVRKLQ 177
Cdd:pfam00210  83 --EVLEAALEHEKKVTKSLRELIELAEEegDYATADFLQW-FLDEQEEHEWFLE 133
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 36-205 2.24e-12

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: 62.66  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  36 TSKCAVAVKGQIQHELNAAFGYMYMGAYFAQYAVDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNI------PNYT 109
Cdd:cd00904     1 SEKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELqdiekpPSDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744 110 FNNNqlntsfvgktrpyKAALEQALNMEIEVTNLIYNVVKECGE--DYHGADVFTNPILDEQHNGVRKLQGAVKTYADLH 187
Cdd:cd00904    81 WGGT-------------LDAMEAALKLEKFVNQALLDLHELASEekDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLN 147

                         170
                  ....*....|....*...
gi 2068667744 188 LNQendeaaAALAEYIFD 205
Cdd:cd00904   148 GQQ------AGSGEYLFD 159
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 47-170 1.39e-04

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: 40.17  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068667744  47 IQHELNAAFGYMYMGAYFaqyavDRPGIAKFLLESATEERSHAIQMLDYLNTRGIKLNIPNYTFNNNQLNTSFVGKtrpY 126
Cdd:cd00657     7 LAGEYAAIIAYGQLAARA-----PDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTSDD---P 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2068667744 127 KAALEQALNMEiEVTNLIYNVVKECGEDYHGADVFTNPILDEQH 170
Cdd:cd00657    79 AEALRAALEVE-ARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH