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Conserved domains on  [gi|1847308381|gb|QKF50089|]
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Bacterioferritin [Pseudomonas graminis]

Protein Classification

bacterioferritin( domain architecture ID 10097036)

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
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 1.67e-78

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: 229.35  E-value: 1.67e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   2 QGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRlGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847308381  81 TVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRiQLADTEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 1.67e-78

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: 229.35  E-value: 1.67e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   2 QGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRlGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847308381  81 TVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRiQLADTEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-153 7.79e-74

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 217.37  E-value: 7.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   3 GHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVGTT 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDlGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847308381  82 VPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADtEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQ 151
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-154 6.31e-48

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: 152.27  E-value: 6.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   1 MQGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRM-RPDDLDVG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847308381  80 TTVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADTEEdHTYWLEKQLGLIKSIGLENYLQSQF 154
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQV 154
PRK10635 PRK10635
bacterioferritin; Provisional
 1-153 6.08e-41

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 134.58  E-value: 6.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   1 MQGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDlGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847308381  80 TTVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADtEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQ 153
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-142 1.82e-34

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: 117.39  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   8 IDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP------DDLDVGTT 81
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRvellaiEAPPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847308381  82 VPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILrIQLADTEEDHTYWLEKQLGLIK 142
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFL-QWFLDEQEEHEWFLEALLEKLE 140
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 2-153 1.67e-78

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: 229.35  E-value: 1.67e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   2 QGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVGT 80
Cdd:cd00907     1 KGDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRlGKLRIGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847308381  81 TVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRiQLADTEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:cd00907    81 DVPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLE-EILEDEEEHIDWLETQLDLIDKMGLQNYLQSQ 152
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-153 7.79e-74

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 217.37  E-value: 7.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   3 GHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVGTT 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQDlGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847308381  82 VPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADtEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQ 151
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-154 6.31e-48

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: 152.27  E-value: 6.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   1 MQGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRM-RPDDLDVG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847308381  80 TTVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADTEEdHTYWLEKQLGLIKSIGLENYLQSQF 154
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQV 154
PRK10635 PRK10635
bacterioferritin; Provisional
 1-153 6.08e-41

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 134.58  E-value: 6.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   1 MQGHPDVIDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP-DDLDVG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDlGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847308381  80 TTVPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILRIQLADtEEDHTYWLEKQLGLIKSIGLENYLQSQ 153
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQ 153
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-142 1.82e-34

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: 117.39  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   8 IDYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERINHEMEEEAQHADALMRRILMLEGTPRMRP------DDLDVGTT 81
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRvellaiEAPPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847308381  82 VPEMLASDLRLEYKVRAALCKGIALCEQHRDYVSRDILrIQLADTEEDHTYWLEKQLGLIK 142
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFL-QWFLDEQEEHEWFLEALLEKLE 140
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 4.25e-11

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: 56.74  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   9 DYLNTLLTGELAARDQYFVHSRMYEDWGFSKLYERInheMEEEAQHADALMRRILMLEGTPRMRPDDLDVGTTVP----- 83
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEI---ADEERRHADALAERLRELGGTPPLPPAHLLAAYALPktsdd 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1847308381  84 --EMLASDLRLEYKVRAALCkgiALCEQHRDYVSRDILRIQLADtEEDHTYWLEKQL 138
Cdd:cd00657    78 paEALRAALEVEARAIAAYR---ELIEQADDPELRRLLERILAD-EQRHAAWFRKLL 130
Euk_Ferritin cd01056
eukaryotic ferritins; Eukaryotic Ferritin (Euk_Ferritin) domain. Ferritins are the primary ...
 4-145 1.54e-05

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: 42.53  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381   4 HPDVIDYLNTLLTGELAARDQYFVHSRMYEDW-----GFSKLYERINHemeEEAQHADALMRRILMLEGT----PRMRPD 74
Cdd:cd01056     1 HEECEAALNKQINLELNASYVYLSMAAYFDRDdvalpGFAKFFRKLSD---EEREHAEKLIKYQNKRGGRvvlqDIKKPE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847308381  75 DLDVGTTVPEMLASdLRLEYKVRAALCKGIALCEQHRDYvsrdilriQLADTEEDHtyWLEKQLGLIKSIG 145
Cdd:cd01056    78 KDEWGSGLEALELA-LDLEKLVNQSLLDLHKLASEHNDP--------HLADFLESE--FLEEQVESIKKLA 137
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 16-95 1.28e-03

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: 37.26  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847308381  16 TGELAARDQYFVHSRMYEDWG--FSKLYERINH-EMeeeaQHADALMRRILMLEGTPRMR-----------PDDLDVGTT 81
Cdd:cd07908    26 NSELTAISQYIYQHLISEEKYpeIAETFLGIAIvEM----HHLEILGQLIVLLGGDPRYRssssdkftywtGKYVNYGES 101

                          90
                  ....*....|....
gi 1847308381  82 VPEMLASDLRLEYK 95
Cdd:cd07908   102 IKEMLKLDIASEKA 115
 
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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