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Conserved domains on  [gi|148281926|gb|ABQ56014|]
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bacterioferritin (cytochrome b1) [Legionella pneumophila str. Corby]

Protein Classification

bacterioferritin( domain architecture ID 10005564)

bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
12-146 4.43e-28

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


:

Pssm-ID: 441796  Cd Length: 152  Bit Score: 101.42  E-value: 4.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  12 DDAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTL-KIGKLLEthEH 90
Cdd:COG2193    2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLqDLGKLRI--GE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148281926  91 NISNILEESLEHERQSLDLYYQLLQYSEN-KSVLVEEFARQMIQEEEMHLGEISKML 146
Cdd:COG2193   80 DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQL 136
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
12-146 4.43e-28

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 101.42  E-value: 4.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  12 DDAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTL-KIGKLLEthEH 90
Cdd:COG2193    2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLqDLGKLRI--GE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148281926  91 NISNILEESLEHERQSLDLYYQLLQYSEN-KSVLVEEFARQMIQEEEMHLGEISKML 146
Cdd:COG2193   80 DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQL 136
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 16-147 7.69e-14

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: 64.23  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926   16 IKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTLKIGKLLETHE----HN 91
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfGS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148281926   92 ISNILEESLEHERQSLDLYYQLLQYS-ENKSVLVEEFARQMIQEEEMHLGEISKMLN 147
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAeEEGDYATADFLQWFLDEQEEHEWFLEALLE 137
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 19-146 2.54e-12

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: 60.20  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  19 LNKLLEIELAGVVRYTHYSFMvfgFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPT-----LKIGKLLETHEHNIS 93
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAAR---APDPDLKDELLEIADEERRHADALAERLRELGGTPPlppahLLAAYALPKTSDDPA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148281926  94 NILEESLEHERQSLDLYYQLLQYSENKsvLVEEFARQMIQEEEMHLGEISKML 146
Cdd:cd00657   80 EALRAALEVEARAIAAYRELIEQADDP--ELRRLLERILADEQRHAAWFRKLL 130
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
12-146 4.43e-28

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 101.42  E-value: 4.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  12 DDAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTL-KIGKLLEthEH 90
Cdd:COG2193    2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLqDLGKLRI--GE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148281926  91 NISNILEESLEHERQSLDLYYQLLQYSEN-KSVLVEEFARQMIQEEEMHLGEISKML 146
Cdd:COG2193   80 DVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQL 136
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 16-147 7.69e-14

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: 64.23  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926   16 IKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTLKIGKLLETHE----HN 91
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfGS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148281926   92 ISNILEESLEHERQSLDLYYQLLQYS-ENKSVLVEEFARQMIQEEEMHLGEISKMLN 147
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAeEEGDYATADFLQWFLDEQEEHEWFLEALLE 137
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 19-146 2.54e-12

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: 60.20  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  19 LNKLLEIELAGVVRYTHYSFMvfgFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPT-----LKIGKLLETHEHNIS 93
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAAR---APDPDLKDELLEIADEERRHADALAERLRELGGTPPlppahLLAAYALPKTSDDPA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148281926  94 NILEESLEHERQSLDLYYQLLQYSENKsvLVEEFARQMIQEEEMHLGEISKML 146
Cdd:cd00657   80 EALRAALEVEARAIAAYRELIEQADDP--ELRRLLERILADEQRHAAWFRKLL 130
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 13-146 7.89e-06

DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a phylogenetically distinct class within the ferritin-like superfamily, and similar in many ways to the DPS (DNA Protecting protein under Starved conditions) proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize hydrogen peroxide in the controlled oxidation of iron, and possess a short N-terminal extension implicated in stabilizing cellular DNA. This domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins are distantly related to bacterial ferritins which assemble 24 monomers, each of which have a four-helix bundle with a fifth shorter helix at the C terminus and a diiron (ferroxidase) center. Ferritins contain a center where oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of iron in the ferric form. Many of the conserved residues of a diiron center are present in this domain.


Pssm-ID: 153111  Cd Length: 148  Bit Score: 43.05  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  13 DAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTLKIGKLLETHEHN- 91
Cdd:cd01052    5 DELIELLNKAFADEWLAYYYYTILAKHVKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEISGCKc 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148281926  92 ---------ISNILEESLEHERQSLDLYYQLLQYSENKSVLVEEFARQMIQEEEMHLGEISKML 146
Cdd:cd01052   85 gylppdppdVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEHEEDLEELL 148
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 13-138 3.39e-05

Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, recombination and repair];


Pssm-ID: 441962  Cd Length: 165  Bit Score: 41.43  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  13 DAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLI--------GELITHFS-YHPTLKIGK 83
Cdd:COG2406   15 DELIELLNKAYADEWLAYYYYWIGAKNVKGLMGEGIKEELEDHAEEELNHAELLaeriyelgGTPPLDPEeWAELSGCGY 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148281926  84 LLETHEHNISNILEESLEHERQSLDLYYQLLQYSENKSVLVEEFARQMIQEEEMH 138
Cdd:COG2406   95 DLPEDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEH 149
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
15-147 2.91e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 35.85  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  15 IIKTLNKLLEIELAGVVRYTHYSFMVfgfNRIPICKWMRDQAQESLNHAHLIGELITHF----------SYHPTLKIGKL 84
Cdd:COG1633    2 LLEILKEAIAMEEEAIEFYLELAEKA---KDPELKKLFEELAEEEKKHAELLEKLYEKLggkpvappeeESQPGLAELMD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148281926  85 LETHEHNISNILEESLEHERQSLDLYYQLLQYSENKSvlVEEFARQMIQEEEMHLGEISKMLN 147
Cdd:COG1633   79 KLDGSVSDAEALELAIATEKDAIEFYRELAAKVGDPE--IKKLFEELAADEKEHAALLEGLYD 139
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 23-146 6.45e-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: 35.02  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148281926  23 LEIELAGvvrYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFS--------------YHPTLKIGKLLETH 88
Cdd:cd01045    7 IKMEEEA---AEFYLELAEKAKDPELKKLFEELAEEEKEHAERLEELYEKLFgeelpelepedykeEVEEEPEFKKALES 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148281926  89 EHNISNILEESLEHERQSLDLYYQLLQYSENKSvlVEEFARQMIQEEEMHLGEISKML 146
Cdd:cd01045   84 LMDPLEALRLAIEIEKDAIEFYEELAEKAEDPE--VKKLFEELAEEERGHLRLLEELY 139
 
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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