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Conserved domains on  [gi|254675294|ref|NP_082322|]
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ferritin heavy polypeptide-like 17 [Mus musculus]

Protein Classification

ferritin family protein( domain architecture ID 10099405)

ferritin family protein such as ferritin, the primary iron storage protein of most living organisms that belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins

CATH:  1.20.1260.10
Gene Ontology:  GO:0005506|GO:0006826|GO:0006879
PubMed:  10441528|20705053|3304136|9444766|8749363
SCOP:  4000839

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 ...
 15-173 9.90e-51

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: 160.40  E-value: 9.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  15 ESNAALNSQIQLQLYGSYIYLSMASFCNKEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQDRQDWL 94
Cdd:cd01056    3 ECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675294  95 DGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVEILKEMGGYMTNLRRLGAPENQDAEKLFDQL 173
Cdd:cd01056   83 SGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDKY 161
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 15-173 9.90e-51

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: 160.40  E-value: 9.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  15 ESNAALNSQIQLQLYGSYIYLSMASFCNKEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQDRQDWL 94
Cdd:cd01056    3 ECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675294  95 DGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVEILKEMGGYMTNLRRLGAPENQDAEKLFDQL 173
Cdd:cd01056   83 SGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDKY 161
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 18-157 2.58e-23

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: 89.65  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294   18 AALNSQIQLQLYGSYIYLSMASFCnkEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRI---ANQDRQDWL 94
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYV--KGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVellAIEAPPSFG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675294   95 DGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKcHFLPQQVEILKEMGGYMTNLRR 157
Cdd:pfam00210  80 SVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
19-159 4.79e-11

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 58.22  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  19 ALNSQIQLQLYGSYIYLSMASFCnkEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQdRQDWLDGLM 98
Cdd:COG1528    9 ALNEQINLEFYSSYLYLAMAAWC--DEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAP-PNEFESLLE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675294  99 AMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKcHFLPQQVEILKEMGGYMTNLRRLG 159
Cdd:COG1528   86 VFEAALEHEQKVTKSINELVDLAREEKDYATENFLQ-WFVKEQVEEEALARTILDKLKLAG 145
PRK10304 PRK10304
non-heme ferritin;
20-143 7.40e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 38.49  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  20 LNSQIQLQLYGSYIYLSMASFCNKEevALGSFALFFLRQSQKWMERTEMLFSLLTErQGSLTlgRIANQD----RQDWLD 95
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTD-TGNLP--RINTVEspfaEYSSLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 254675294  96 GLmaMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVE 143
Cdd:PRK10304  85 EL--FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEE 130
 
Name Accession Description Interval E-value
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 15-173 9.90e-51

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: 160.40  E-value: 9.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  15 ESNAALNSQIQLQLYGSYIYLSMASFCNKEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQDRQDWL 94
Cdd:cd01056    3 ECEAALNKQINLELNASYVYLSMAAYFDRDDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEKDEWG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675294  95 DGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVEILKEMGGYMTNLRRLGAPENQDAEKLFDQL 173
Cdd:cd01056   83 SGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESEFLEEQVESIKKLAGYITNLKRVGKPQSGLGEYLFDKY 161
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 14-172 2.07e-39

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: 131.61  E-value: 2.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  14 SESNAALNSQIQLQLYGSYIYLSMASFCNKEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQDRQDW 93
Cdd:cd00904    2 EKVEAAVNRQLNLELYASYTYLSMATYFDRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPSDEW 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675294  94 LDGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVEILKEMGGYMTNLRRLGAPENQDAEKLFDQ 172
Cdd:cd00904   82 GGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLESHFLDEQVKEIKQVGDILTNLERLNGQQAGSGEYLFDR 160
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 18-157 2.58e-23

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: 89.65  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294   18 AALNSQIQLQLYGSYIYLSMASFCnkEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRI---ANQDRQDWL 94
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYV--KGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVellAIEAPPSFG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675294   95 DGLMAMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKcHFLPQQVEILKEMGGYMTNLRR 157
Cdd:pfam00210  80 SVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQ-WFLDEQEEHEWFLEALLEKLER 141
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 19-159 4.48e-15

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: 68.67  E-value: 4.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  19 ALNSQIQLQLYGSYIYLSMASFCNKEEvaLGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIAnQDRQDWLDGLM 98
Cdd:cd01055    7 ALNEQINLELYSSYLYLAMAAWFDSKG--LDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIE-APPSEFESLLE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675294  99 AMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKcHFLPQQVEILKEMGGYMTNLRRLG 159
Cdd:cd01055   84 VFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQ-WFVKEQVEEEALARDILDKLKLAG 143
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
19-159 4.79e-11

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 58.22  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  19 ALNSQIQLQLYGSYIYLSMASFCnkEEVALGSFALFFLRQSQKWMERTEMLFSLLTERQGSLTLGRIANQdRQDWLDGLM 98
Cdd:COG1528    9 ALNEQINLEFYSSYLYLAMAAWC--DEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAP-PNEFESLLE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675294  99 AMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKcHFLPQQVEILKEMGGYMTNLRRLG 159
Cdd:COG1528   86 VFEAALEHEQKVTKSINELVDLAREEKDYATENFLQ-WFVKEQVEEEALARTILDKLKLAG 145
PRK10304 PRK10304
non-heme ferritin;
20-143 7.40e-04

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 38.49  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675294  20 LNSQIQLQLYGSYIYLSMASFCNKEevALGSFALFFLRQSQKWMERTEMLFSLLTErQGSLTlgRIANQD----RQDWLD 95
Cdd:PRK10304  10 LNEQMNLELYSSLLYQQMSAWCSYH--TFEGAAAFLRRHAQEEMTHMQRLFDYLTD-TGNLP--RINTVEspfaEYSSLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 254675294  96 GLmaMECAFHLEKTLNQSLLQLYGLANSKGDLYLCNFLKCHFLPQQVE 143
Cdd:PRK10304  85 EL--FQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEE 130
 
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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