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Conserved domains on  [gi|183178687|gb|ACC43797|]
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bacterioferritin BfrB [Mycobacterium marinum M]

Protein Classification

ferritin( domain architecture ID 10003944)

non-heme ferritin is an iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
23-175 4.33e-59

Ferritin [Inorganic ion transport and metabolism];


:

Pssm-ID: 441137  Cd Length: 158  Bit Score: 182.25  E-value: 4.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRNHFDK 102
Cdd:COG1528    3 SEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEFES 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183178687 103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLVRIADRAG---ANLFELENFV 175
Cdd:COG1528   83 LLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDKLKLAGddgSGLFMLDKEL 158
 
Name Accession Description Interval E-value
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
23-175 4.33e-59

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 182.25  E-value: 4.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRNHFDK 102
Cdd:COG1528    3 SEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEFES 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183178687 103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLVRIADRAG---ANLFELENFV 175
Cdd:COG1528   83 LLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDKLKLAGddgSGLFMLDKEL 158
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 25-175 1.37e-49

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: 158.03  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  25 KFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRNHFDKPR 104
Cdd:cd01055    3 KLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEFESLL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 183178687 105 DALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASL---VRIADRAGANLFELENFV 175
Cdd:cd01055   83 EVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQWFVKEQVEEEALARDIldkLKLAGDDGGGLYMLDKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 28-163 3.63e-30

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: 107.76  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687   28 ALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRD-----LRVEIPGIDSVrNHFDK 102
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGgtpngTRVELLAIEAP-PSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183178687  103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLVRIADR 163
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
PRK10304 PRK10304
non-heme ferritin;
23-179 6.95e-06

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 44.27  E-value: 6.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDlrvEIPGIDSVRNHFDK 102
Cdd:PRK10304   3 KPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTG---NLPRINTVESPFAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687 103 --PRDALALA-LDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLV---RIADRAGANLFelenFVA 176
Cdd:PRK10304  80 ysSLDELFQEtYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIdklSLAGKSGEGLY----FID 155


                 ...
gi 183178687 177 REV 179
Cdd:PRK10304 156 KEL 158
 
Name Accession Description Interval E-value
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
23-175 4.33e-59

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 182.25  E-value: 4.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRNHFDK 102
Cdd:COG1528    3 SEKMEKALNEQINLEFYSSYLYLAMAAWCDEKGLPGFANFFRVQAQEERTHAMKFFDYLNDRGGRVELPAIDAPPNEFES 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183178687 103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLVRIADRAG---ANLFELENFV 175
Cdd:COG1528   83 LLEVFEAALEHEQKVTKSINELVDLAREEKDYATENFLQWFVKEQVEEEALARTILDKLKLAGddgSGLFMLDKEL 158
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 25-175 1.37e-49

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: 158.03  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  25 KFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRNHFDKPR 104
Cdd:cd01055    3 KLEKALNEQINLELYSSYLYLAMAAWFDSKGLDGFANFFRVQAQEEREHAMKFFDYLNDRGGRVELPAIEAPPSEFESLL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 183178687 105 DALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASL---VRIADRAGANLFELENFV 175
Cdd:cd01055   83 EVFEAALEHEQKVTESINNLVDLALEEKDYATFNFLQWFVKEQVEEEALARDIldkLKLAGDDGGGLYMLDKEL 156
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 28-163 3.63e-30

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: 107.76  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687   28 ALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRD-----LRVEIPGIDSVrNHFDK 102
Cdd:pfam00210   2 AALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGgtpngTRVELLAIEAP-PSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183178687  103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLVRIADR 163
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKLER 141
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 28-149 9.27e-16

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: 71.04  E-value: 9.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  28 ALVQEQIFNEFTAAQQYVAIAVYFDGEE--LPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDS-VRNHFDKPR 104
Cdd:cd01056    6 AALNKQINLELNASYVYLSMAAYFDRDDvaLPGFAKFFRKLSDEEREHAEKLIKYQNKRGGRVVLQDIKKpEKDEWGSGL 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 183178687 105 DALALALDQERAVTDQVSRLTAVARDESD-----FLGEQfmqwFLQEQIE 149
Cdd:cd01056   86 EALELALDLEKLVNQSLLDLHKLASEHNDphladFLESE----FLEEQVE 131
Ferritin cd00904
Ferritin iron storage proteins; Ferritins are the primary iron storage proteins of most living ...
 24-165 1.54e-11

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: 59.97  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  24 TKFHALVQEQIFNEFTAAQQYVAIAVYFDGEE--LPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDS-VRNHF 100
Cdd:cd00904    2 EKVEAAVNRQLNLELYASYTYLSMATYFDRDDvaLKGVAHFFKEQAQEEREHAEKFYKYQNERGGRVELQDIEKpPSDEW 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183178687 101 DKPRDALALALDQERAVTDQVSRLTAVARDESDFLGEQFMQW-FLQEQIEEVALMASLVRIADRAG 165
Cdd:cd00904   82 GGTLDAMEAALKLEKFVNQALLDLHELASEEKDPHLCDFLEShFLDEQVKEIKQVGDILTNLERLN 147
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
23-150 4.59e-06

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 44.41  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDLRVEIPGIDSVRnHFDK 102
Cdd:COG2193    2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLR-IGED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 183178687 103 PRDALALALDQERAVTDQVSRLTAVARDESDFLGEQfmqwFLQEQIEE 150
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRD----LLEEILED 124
PRK10304 PRK10304
non-heme ferritin;
23-179 6.95e-06

non-heme ferritin;


Pssm-ID: 182367  Cd Length: 165  Bit Score: 44.27  E-value: 6.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  23 KTKFHALVQEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAMMLVQHLIDRDlrvEIPGIDSVRNHFDK 102
Cdd:PRK10304   3 KPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTG---NLPRINTVESPFAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687 103 --PRDALALA-LDQERAVTDQVSRLTAVARDESDFLGEQFMQWFLQEQIEEVALMASLV---RIADRAGANLFelenFVA 176
Cdd:PRK10304  80 ysSLDELFQEtYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIdklSLAGKSGEGLY----FID 155


                 ...
gi 183178687 177 REV 179
Cdd:PRK10304 156 KEL 158
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 31-134 4.38e-03

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: 35.98  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183178687  31 QEQIFNEFTAAQQYVAIAVYFDGEELPQLAKHFYAQAVEERNHAmmlvQHLIDRDLRVEipGIDSVRNHfDKPRDA---- 106
Cdd:cd00907   11 NKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHA----DKLIERILFLE--GLPNLQRL-GKLRIGedvp 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 183178687 107 --LALALDQERAVTDQVSRLTAVARDESDF 134
Cdd:cd00907   84 emLENDLALEYEAIAALNEAIALCEEVGDY 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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