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Conserved domains on  [gi|685661515|gb|AIO48642|]
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bacterioferritin [Burkholderia cepacia]

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];
3-154 4.76e-88

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


:

Pssm-ID: 441796  Cd Length: 152  Bit Score: 253.58  E-value: 4.76e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   3 GDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGEE 82
Cdd:COG2193    1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685661515  83 TEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 4.76e-88

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 253.58  E-value: 4.76e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   3 GDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGEE 82
Cdd:COG2193    1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685661515  83 TEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 2.47e-84

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: 244.38  E-value: 2.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   2 QGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGE 81
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685661515  82 ETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:cd00907   81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 5.17e-72

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 213.52  E-value: 5.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515    1 MQGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685661515   81 EETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMMGSP 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
PRK10635 PRK10635
bacterioferritin; Provisional
 1-154 4.53e-66

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 198.52  E-value: 4.53e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   1 MQGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685661515  81 EETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQI 154
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-141 5.84e-36

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: 121.24  E-value: 5.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515    8 IEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGE-----E 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 685661515   83 TEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLI 141
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKL 139
 
Name Accession Description Interval E-value
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 4.76e-88

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 253.58  E-value: 4.76e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   3 GDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGEE 82
Cdd:COG2193    1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDLGKLRIGED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685661515  83 TEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:COG2193   81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLELIEKIGLQNYLQSQM 152
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-154 2.47e-84

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: 244.38  E-value: 2.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   2 QGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGE 81
Cdd:cd00907    1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRIGE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685661515  82 ETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:cd00907   81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-157 5.17e-72

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 213.52  E-value: 5.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515    1 MQGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVG 80
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685661515   81 EETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMMGSP 157
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEEHIDWLETQLELIDKLGLENYLQAQVSEE 157
PRK10635 PRK10635
bacterioferritin; Provisional
 1-154 4.53e-66

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 198.52  E-value: 4.53e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   1 MQGDKKVIEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVG 80
Cdd:PRK10635   1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLNIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685661515  81 EETEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLIGKVGLQNYQQTMM 154
Cdd:PRK10635  81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIGKLGLQNYLQSQI 154
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-141 5.84e-36

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: 121.24  E-value: 5.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515    8 IEYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDESIGEMKHADWLIERVFMLDGLPNLQDLHKLLVGE-----E 82
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAppsfgS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 685661515   83 TEEILKCDLKLEQISQSTCKEAIAYCESVRDYVSREIFEKILDDTEEHIDWLETQIDLI 141
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALLEKL 139
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-136 7.81e-14

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: 64.05  E-value: 7.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   9 EYLNAQLKNELTAINQYFLHARMYKHWGLDKLGKHEYDEsigEMKHADWLIERVFMLDGLPNLQDLHKLLVGEET----- 83
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADE---ERRHADALAERLRELGGTPPLPPAHLLAAYALPktsdd 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 685661515  84 -EEILKCDLKLEQISQSTCKEAIAYCEsvrDYVSREIFEKILDDTEEHIDWLET 136
Cdd:cd00657   78 pAEALRAALEVEARAIAAYRELIEQAD---DPELRRLLERILADEQRHAAWFRK 128
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 5-136 2.80e-07

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: 47.28  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   5 KKVIEYLNAQLKNELTAINQYFLHARMYKhwGLDKLG-KHEYDES-IGEMKHADWLIERVFMLDGLP--NLQDLHKLLVG 80
Cdd:cd01052    5 DELIELLNKAFADEWLAYYYYTILAKHVK--GPEGEGiKEELEEAaEEELNHAELLAERIYELGGTPprDPKDWYEISGC 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685661515  81 E---------ETEEILKCDLKLEQISQSTCKEAIAYCESvRDYVSREIFEKILDDTEEHIDWLET 136
Cdd:cd01052   83 KcgylppdppDVKGILKVNLKAERCAIKVYKELCDMTHG-KDPVTYDLALAILNEEIEHEEDLEE 146
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 5-136 3.64e-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: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   5 KKVIEYLNAQLKNELTAINQYFLHARMYKhwGLDKLG-KHEYDES-IGEMKHADWLIERVFMLDGLP--NLQDLHKL--- 77
Cdd:COG2406   15 DELIELLNKAYADEWLAYYYYWIGAKNVK--GLMGEGiKEELEDHaEEELNHAELLAERIYELGGTPplDPEEWAELsgc 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685661515  78 ---LVGEET--EEILKCDLKLEQISQSTCKEAIAYCESVrDYVSREIFEKILDDTEEHIDWLET 136
Cdd:COG2406   93 gydLPEDPTdvRAILEQNLKAERCAIKVYNELCNMTKGK-DPVTYDLALDILEEEVEHEQDLED 155
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
6-141 4.58e-05

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 40.86  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515   6 KVIEYLNAQLKNELTAINQYFLHARMYKhwglDKLGKHEYDE-SIGEMKHADWLIERVFMLDG----------LPNLQDL 74
Cdd:COG1633    1 SLLEILKEAIAMEEEAIEFYLELAEKAK----DPELKKLFEElAEEEKKHAELLEKLYEKLGGkpvappeeesQPGLAEL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685661515  75 HKLLVGEETE-EILKCDLKLEQISQSTCKEAIaycESVRDYVSREIFEKILDDTEEHIDWLETQIDLI 141
Cdd:COG1633   77 MDKLDGSVSDaEALELAIATEKDAIEFYRELA---AKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 18-138 2.35e-04

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: 39.18  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685661515  18 ELTAINQYFlharmYKHWGLDKlgkhEYDE--------SIGEMKHADWLIERVFMLDGLPNLQDLHK----------LLV 79
Cdd:cd07908   28 ELTAISQYI-----YQHLISEE----KYPEiaetflgiAIVEMHHLEILGQLIVLLGGDPRYRSSSSdkftywtgkyVNY 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 685661515  80 GEETEEILKCDLKLEQISQSTCKEAIAYcesVRDYVSREIFEKILDDTEEHIDWLETQI 138
Cdd:cd07908   99 GESIKEMLKLDIASEKAAIAKYKRQAET---IKDPYIRALLNRIILDEKLHIKILEELL 154
 
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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