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Conserved domains on  [gi|2775737309|ref|WP_367651452|]
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ferritin-like domain-containing protein [Cupriavidus basilensis]

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, ...
 72-187 5.85e-09

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: 53.27  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  72 YYAANPEASGWLsEHWEAEELQHGLALRRYVEHVWPEFDWERGYARFFEEyrhtcsiDKFEPTKALEM-AARCVVETGTA 150
Cdd:cd00657    22 ARAPDPDLKDEL-LEIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEAlRAALEVEARAI 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2775737309 151 ALYRSLEQASDEPVLRNLTRRIADDEVRHYKHFYRYF 187
Cdd:cd00657    94 AAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 72-187 5.85e-09

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: 53.27  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  72 YYAANPEASGWLsEHWEAEELQHGLALRRYVEHVWPEFDWERGYARFFEEyrhtcsiDKFEPTKALEM-AARCVVETGTA 150
Cdd:cd00657    22 ARAPDPDLKDEL-LEIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEAlRAALEVEARAI 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2775737309 151 ALYRSLEQASDEPVLRNLTRRIADDEVRHYKHFYRYF 187
Cdd:cd00657    94 AAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
85-188 2.62e-05

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 43.17  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  85 EHWEAEELQHGLALRRYVEHVW--PEFDWERGYARFFEEYRHTCSIDKfEPTKALEMAARcvVETGTAALYRSLEQASDE 162
Cdd:COG1633    37 EELAEEEKKHAELLEKLYEKLGgkPVAPPEEESQPGLAELMDKLDGSV-SDAEALELAIA--TEKDAIEFYRELAAKVGD 113

                          90       100
                  ....*....|....*....|....*.
gi 2775737309 163 PVLRNLTRRIADDEVRHYKHFYRYFN 188
Cdd:COG1633   114 PEIKKLFEELAADEKEHAALLEGLYD 139
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 72-187 5.85e-09

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: 53.27  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  72 YYAANPEASGWLsEHWEAEELQHGLALRRYVEHVWPEFDWERGYARFFEEyrhtcsiDKFEPTKALEM-AARCVVETGTA 150
Cdd:cd00657    22 ARAPDPDLKDEL-LEIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEAlRAALEVEARAI 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2775737309 151 ALYRSLEQASDEPVLRNLTRRIADDEVRHYKHFYRYF 187
Cdd:cd00657    94 AAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
85-188 2.62e-05

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 43.17  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  85 EHWEAEELQHGLALRRYVEHVW--PEFDWERGYARFFEEYRHTCSIDKfEPTKALEMAARcvVETGTAALYRSLEQASDE 162
Cdd:COG1633    37 EELAEEEKKHAELLEKLYEKLGgkPVAPPEEESQPGLAELMDKLDGSV-SDAEALELAIA--TEKDAIEFYRELAAKVGD 113

                          90       100
                  ....*....|....*....|....*.
gi 2775737309 163 PVLRNLTRRIADDEVRHYKHFYRYFN 188
Cdd:COG1633   114 PEIKKLFEELAADEKEHAALLEGLYD 139
Acyl_ACP_Desat cd01050
Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase ...
 77-252 4.77e-05

Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase (Acyl_ACP_Desat) is a mu-oxo-bridged diiron-carboxylate enzyme, which belongs to a broad superfamily of ferritin-like proteins and catalyzes the NADPH and O2-dependent formation of a cis-double bond in acyl-ACPs. Acyl-ACP desaturases are found in higher plants and a few bacterial species (Mycobacterium tuberculosis, M. leprae, M. avium and Streptomyces avermitilis, S. coelicolor). In plants, Acyl-ACP desaturase is a plastid-localized, covalently ACP linked, soluble desaturase that introduces the first double bound into saturated fatty acids, resulting in the corresponding monounsaturated fatty acid. Members of this class of soluble desaturases are specific for a particular substrate chain length and introduce the double bond between specific carbon atoms. For example, delta 9 stearoyl-ACP is specific for stearic acid and introduces a double bond between carbon 9 and 10 to yield oleic acid in the ACP-bound form. The enzymatic reaction requires molecular oxygen, NAD(P)H, NAD(P)H ferredoxin oxido-reductase and ferredoxin. The enzyme is active in the homodimeric form; the monomer consists mainly of alpha-helices with the catalytic diiron center buried within a four-helix bundle. Integral membrane fatty acid desaturases that introduce double bonds into fatty acid chains, acyl-CoA desaturases of animals, yeasts, and fungi, and acyl-lipid desaturases of cyanobacteria and higher plants, are distinct from soluble acyl-ACP desaturases, lack diiron centers, and are not included in this CD.


Pssm-ID: 153109  Cd Length: 297  Bit Score: 44.18  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309  77 PEASGW--LSEHWEAEELQHGLALRRYVehvwpeFDWERGYARFFEEYRHTCSIDKFEPTK----ALEMAARCVVETGTA 150
Cdd:cd01050    90 ESPTAWarWVRRWTAEENRHGDLLNKYL------YLTGRVDPRALERTRQYLIGSGFDPGTdnspYRGFVYTSFQELATR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309 151 ALYRSLEQASD--EPVLRNLTRRIADDEVRHYKhFYRYFntfngverlgrlrvlgalVRRLLEIKNEDAEIALRNVLRIE 228
Cdd:cd01050   164 ISHRNTARLAGagDPVLAKLLGRIAADEARHEA-FYRDI------------------VEALFELDPDGAVLAFADMMRKI 224

                         170       180
                  ....*....|....*....|....
gi 2775737309 229 RgtedIPQRDVRKLNSRVSAVIRR 252
Cdd:cd01050   225 V----MPGHLMYPLFERFAAVAAR 244
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
132-192 3.36e-04

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 40.09  E-value: 3.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2775737309 132 EPTKALEMAARcvVETGTAALYRSLEQASDEPVLRNLTRRIADDEVRHYKHFYRYFNTFNG 192
Cdd:COG1633     1 SLLEILKEAIA--MEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGG 59
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 136-227 1.84e-03

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: 37.71  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2775737309 136 ALEMAARcvVETGTAALYRSLEQASDEPVLRNLTRRIADDEVRHYKHFYRYFNTFNGVE--RLGRLRVLGALVRRLLEIK 213
Cdd:cd01045     2 ILALAIK--MEEEAAEFYLELAEKAKDPELKKLFEELAEEEKEHAERLEELYEKLFGEElpELEPEDYKEEVEEEPEFKK 79

                          90
                  ....*....|....
gi 2775737309 214 NEDAEIALRNVLRI 227
Cdd:cd01045    80 ALESLMDPLEALRL 93
 
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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