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Conserved domains on  [gi|446209546|ref|WP_000287401|]
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MULTISPECIES: ferritin-like domain-containing protein [Bacillus]

Protein Classification

ferritin-like domain-containing protein( domain architecture ID 10090058)

ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers

CATH:  1.20.1260.10
Gene Ontology:  GO:0046872
PubMed:  8749363|9444766|3304136
SCOP:  3001658

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 18-140 5.38e-33

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: 112.97  E-value: 5.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  18 RDIEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPKP-------QITEECSNTYLQ 90
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPpahllaaYALPKTSDDPAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446209546  91 GLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYF 140
Cdd:cd00657   81 ALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 18-140 5.38e-33

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: 112.97  E-value: 5.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  18 RDIEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPKP-------QITEECSNTYLQ 90
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPpahllaaYALPKTSDDPAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446209546  91 GLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYF 140
Cdd:cd00657   81 ALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
15-143 3.60e-28

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 100.95  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  15 KLIRDIEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPK-------PQITEEC--- 84
Cdd:COG1633    1 SLLEILKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAppeeesqPGLAELMdkl 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446209546  85 --SNTYLQGLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYFVKM 143
Cdd:COG1633   81 dgSVSDAEALELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 18-140 5.38e-33

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: 112.97  E-value: 5.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  18 RDIEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPKP-------QITEECSNTYLQ 90
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPpahllaaYALPKTSDDPAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446209546  91 GLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYF 140
Cdd:cd00657   81 ALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
15-143 3.60e-28

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 100.95  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  15 KLIRDIEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPK-------PQITEEC--- 84
Cdd:COG1633    1 SLLEILKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAppeeesqPGLAELMdkl 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446209546  85 --SNTYLQGLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYFVKM 143
Cdd:COG1633   81 dgSVSDAEALELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 20-132 3.13e-11

Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like domain found in archaea and bacteria (Ferritin_like_AB). This uncharacterized domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins whose function is unknown. This family includes unknown or hypothetical proteins which were sequenced from mostly anaerobic or microaerophilic metal-metabolizing and/or nitrogen-fixing microbes. The family includes sequences from ferric-, sulfate-, and arsenic-reducing bacteria, Geobacter, Magnetospirillum, Desulfovibrio, and Desulfitobacterium. Also included are several nitrogen-fixing endosymbiotic bacteria, Rhizobium, Mesorhizobium, and Bradyrhizobium; also phototrophic purple nonsulfur bacteria, Rhodobacter and Rhodopseudomonas, as well as, obligate thermophiles, Thermotoga, Thermoanaerobacter, and Pyrococcus. The conserved residues of a diiron center are present in this uncharacterized domain.


Pssm-ID: 153104  Cd Length: 139  Bit Score: 56.97  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  20 IEKAINGEFSAINCYAKLANMAPNTVERNQILEIRNDEIKHFHQFVQIYTNLTGQQPKPQITEECSN------------- 86
Cdd:cd01045    3 LALAIKMEEEAAEFYLELAEKAKDPELKKLFEELAEEEKEHAERLEELYEKLFGEELPELEPEDYKEeveeepefkkale 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446209546  87 ---TYLQGLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNH 132
Cdd:cd01045   83 slmDPLEALRLAIEIEKDAIEFYEELAEKAEDPEVKKLFEELAEEERGH 131
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 92-137 5.48e-07

Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like domain found in archaea and bacteria (Ferritin_like_AB). This uncharacterized domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins whose function is unknown. This family includes unknown or hypothetical proteins which were sequenced from mostly anaerobic or microaerophilic metal-metabolizing and/or nitrogen-fixing microbes. The family includes sequences from ferric-, sulfate-, and arsenic-reducing bacteria, Geobacter, Magnetospirillum, Desulfovibrio, and Desulfitobacterium. Also included are several nitrogen-fixing endosymbiotic bacteria, Rhizobium, Mesorhizobium, and Bradyrhizobium; also phototrophic purple nonsulfur bacteria, Rhodobacter and Rhodopseudomonas, as well as, obligate thermophiles, Thermotoga, Thermoanaerobacter, and Pyrococcus. The conserved residues of a diiron center are present in this uncharacterized domain.


Pssm-ID: 153104  Cd Length: 139  Bit Score: 45.80  E-value: 5.48e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446209546  92 LEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFL 137
Cdd:cd01045    3 LALAIKMEEEAAEFYLELAEKAKDPELKKLFEELAEEEKEHAERLE 48
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 15-133 7.52e-07

Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. 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: 153117  Cd Length: 154  Bit Score: 45.73  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  15 KLIRDIEKAINGEFSAINCYaklanmapntVERNQILEIRNDEI------------KHFHQFVQIYTNLTGQQPKPQITE 82
Cdd:cd07908   16 ELLLDDYAGTNSELTAISQY----------IYQHLISEEKYPEIaetflgiaivemHHLEILGQLIVLLGGDPRYRSSSS 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446209546  83 EC-----------SNTYLQGLEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHA 133
Cdd:cd07908   86 DKftywtgkyvnyGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRIILDEKLHI 147
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 92-142 1.86e-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: 39.02  E-value: 1.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446209546  92 LEFAIQDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHAVWFLYYFVK 142
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRE 53
Ferritin_CCC1_N cd01044
Ferritin-CCC1, N-terminal ferritin-like diiron-binding domain; Ferritin-like N-terminal domain ...
 97-135 4.93e-03

Ferritin-CCC1, N-terminal ferritin-like diiron-binding domain; Ferritin-like N-terminal domain present in an uncharacterized family of proteins found in bacteria and archaea. These proteins also have a C-terminal CCC1-like transmembrane domain and are thought to be involved in iron and/or manganese transport. This domain has the conserved residues of a diiron center found in other ferritin-like proteins.


Pssm-ID: 153103  Cd Length: 125  Bit Score: 34.91  E-value: 4.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446209546  97 QDEQKTVDFYLEIADETSDTHLKELLRRIAADEQNHA-VW 135
Cdd:cd01044    8 KDEITEAAIYRKLAKREKDPENREILLKLAEDERRHAeFW 47
Ferritin_CCC1_N cd01044
Ferritin-CCC1, N-terminal ferritin-like diiron-binding domain; Ferritin-like N-terminal domain ...
 34-133 9.53e-03

Ferritin-CCC1, N-terminal ferritin-like diiron-binding domain; Ferritin-like N-terminal domain present in an uncharacterized family of proteins found in bacteria and archaea. These proteins also have a C-terminal CCC1-like transmembrane domain and are thought to be involved in iron and/or manganese transport. This domain has the conserved residues of a diiron center found in other ferritin-like proteins.


Pssm-ID: 153103  Cd Length: 125  Bit Score: 34.14  E-value: 9.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446209546  34 YAKLANMAPNTVERNQILEIRNDEIKHFhqfvQIYTNLTGQQPKPQITEECSNTYLQ------GLEFAIQ----DEQKTV 103
Cdd:cd01044   17 YRKLAKREKDPENREILLKLAEDERRHA----EFWKKFLGKRGVPPPRPKLKIFFYKllarifGPTFVLKllerGEERAI 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 446209546 104 DFYLEIADEtsdthlKELLRRIAADEQNHA 133
Cdd:cd01044   93 EKYDRLLEE------RPELKEIIADELEHE 116
 
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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