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Conserved domains on  [gi|505190379|ref|WP_015377481|]
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MULTISPECIES: non-heme ferritin [Serratia]

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

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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, ...
 1-161 1.22e-87

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 PRK10304:

Pssm-ID: 469698  Cd Length: 165  Bit Score: 253.81  E-value: 1.22e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:PRK10304   1 MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDLKK 160
Cdd:PRK10304  81 SSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELST 160


                 .
gi 505190379 161 M 161
Cdd:PRK10304 161 L 161
 
Name Accession Description Interval E-value
PRK10304 PRK10304
non-heme ferritin;
1-161 1.22e-87

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 253.81  E-value: 1.22e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:PRK10304   1 MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDLKK 160
Cdd:PRK10304  81 SSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELST 160


                 .
gi 505190379 161 M 161
Cdd:PRK10304 161 L 161
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
1-158 5.75e-85

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 246.58  E-value: 5.75e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:COG1528    1 MLSEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDL 158
Cdd:COG1528   81 ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDKLKLAGDDGSGLFMLDKEL 158
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 3-158 1.38e-76

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: 225.44  E-value: 1.38e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   3 TQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAFES 82
Cdd:cd01055    1 SEKLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEFES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190379  83 LADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDL 158
Cdd:cd01055   81 LLEVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQWFVKEQVEEEALARDILDKLKLAGDDGGGLYMLDKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 8.26e-40

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: 131.64  E-value: 8.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379    8 QKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIA----APPVAFESL 83
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVEllaiEAPPSFGSV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   84 ADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLAL 143
Cdd:pfam00210  82 LEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
 
Name Accession Description Interval E-value
PRK10304 PRK10304
non-heme ferritin;
1-161 1.22e-87

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 253.81  E-value: 1.22e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:PRK10304   1 MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDLKK 160
Cdd:PRK10304  81 SSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELST 160


                 .
gi 505190379 161 M 161
Cdd:PRK10304 161 L 161
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
1-158 5.75e-85

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 246.58  E-value: 5.75e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:COG1528    1 MLSEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDL 158
Cdd:COG1528   81 ESLLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDKLKLAGDDGSGLFMLDKEL 158
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 3-158 1.38e-76

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: 225.44  E-value: 1.38e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   3 TQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAFES 82
Cdd:cd01055    1 SEKLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEFES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190379  83 LADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLALVGTSGKGLFFIDKDL 158
Cdd:cd01055   81 LLEVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQWFVKEQVEEEALARDILDKLKLAGDDGGGLYMLDKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 8.26e-40

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: 131.64  E-value: 8.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379    8 QKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIA----APPVAFESL 83
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVEllaiEAPPSFGSV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   84 ADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKLAL 143
Cdd:pfam00210  82 LEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
PRK15022 PRK15022
non-heme ferritin-like protein;
1-141 3.99e-33

non-heme ferritin-like protein;


Pssm-ID: 184983  Cd Length: 167  Bit Score: 115.36  E-value: 3.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAF 80
Cdd:PRK15022   1 MATAGMLLKLNSQMNLEFYASNLYLHLSEWCSEQSLNGTATFLRAQAQSNVTQMMRMFNFMKSAGATPIVKAIDVPGEKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEQHEEEKLFKSVLDKL 141
Cdd:PRK15022  81 NSLEELFQKTLEEYEQRSSTLAQLADEAKALNDDSTLNFLRDLEKEQQHDGLLLQTILDEV 141
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 3-156 9.64e-20

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: 80.77  E-value: 9.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   3 TQEMTQKLNEQLNLEFYSANLYLQMSAW--CSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPP-VA 79
Cdd:cd00904    1 SEKVEAAVNRQLNLELYASYTYLSMATYfdRDDVALKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKPPsDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379  80 FESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQW-YVAEQHEEEKLFKSVLDKLALVGTS--GKGLFFIDK 156
Cdd:cd00904   81 WGGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLEShFLDEQVKEIKQVGDILTNLERLNGQqaGSGEYLFDR 160
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 4-151 1.59e-11

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: 59.09  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   4 QEMTQKLNEQLNLEFYSANLYLQMSAWCS--DKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPP-VAF 80
Cdd:cd01056    2 EECEAALNKQINLELNASYVYLSMAAYFDrdDVALPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKPEkDEW 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190379  81 ESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQW-YVAEQHEEEKLFKSVLDKLALVGTSGKGL 151
Cdd:cd01056   82 GSGLEALELALDLEKLVNQSLLDLHKLASEHNDPHLADFLESeFLEEQVESIKKLAGYITNLKRVGKPQSGL 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
8-131 1.44e-09

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 53.66  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   8 QKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLPLLGTIAAPPVAfESLADVF 87
Cdd:COG2193    7 ELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIG-EDVEEML 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505190379  88 QQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQWYVAEqhEEE 131
Cdd:COG2193   86 ECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED--EEE 127
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 1-121 8.28e-04

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: 37.91  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379   1 MLTQEMTQKLNEQLNLEFYSANLYLQMSAWCSDKGFEGAAAFLKEHSQEEMQHMQRLFD---YLsdtGSLPLLGTIAAPP 77
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIErilFL---EGLPNLQRLGKLR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505190379  78 VAfESLADVFQQTYEHEQLITRQINELAHAAMTAHDYSTFNFLQ 121
Cdd:cd00907   78 IG-EDVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLE 120
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 10-105 1.61e-03

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: 36.71  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190379  10 LNEQLNLEFYSANLYLQMSAwcsDKGFEGAAAFLKEHSQEEMQHMQRLFDYLSDTGSLP-----LLGTIAAPPVAFESLA 84
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAA---RAPDPDLKDELLEIADEERRHADALAERLRELGGTPplppaHLLAAYALPKTSDDPA 79

                         90       100
                 ....*....|....*....|.
gi 505190379  85 DVFQQTYEHEQLITRQINELA 105
Cdd:cd00657   80 EALRAALEVEARAIAAYRELI 100
 
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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