NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1922990879|gb|QOU72589|]
View 

Ferritin-like domain protein [Janthinobacterium sp. HH102]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DPS super family cl42345
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 36-178 4.20e-30

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


The actual alignment was detected with superfamily member COG2406:

Pssm-ID: 441962  Cd Length: 165  Bit Score: 107.68  E-value: 4.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  36 DRQELITLLNGALATELVCIarykrHYYT-----VSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLL 110
Cdd:COG2406    13 DVDELIELLNKAYADEWLAY-----YYYWigaknVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 111 ARSHAEYD---DSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:COG2406    88 ELSGCGYDlpeDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLG 158
 
Name Accession Description Interval E-value
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 36-178 4.20e-30

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 107.68  E-value: 4.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  36 DRQELITLLNGALATELVCIarykrHYYT-----VSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLL 110
Cdd:COG2406    13 DVDELIELLNKAYADEWLAY-----YYYWigaknVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 111 ARSHAEYD---DSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:COG2406    88 ELSGCGYDlpeDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLG 158
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 43-177 3.10e-25

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: 94.49  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  43 LLNGALATELVCIARYKRHYYTVSGRDngtIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLArSHAEYDDSED 122
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAPDPD---LKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLA-AYALPKTSDD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1922990879 123 VQSMVRANLIAERVAIESYRQMIVKIGdkDPTTRHLLIKIMAVEEEHADDMRDLM 177
Cdd:cd00657    78 PAEALRAALEVEARAIAAYRELIEQAD--DPELRRLLERILADEQRHAAWFRKLL 130
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 41-178 1.10e-19

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: 80.41  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  41 ITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLArsHAEYDDS 120
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLA--IEAPPSF 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1922990879 121 EDVQSMVRANLIAERVAIESYRQMI-VKIGDKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIeLAEEEGDYATADFLQWFLDEQEEHEWFLEALLE 137
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
38-178 6.55e-10

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 55.34  E-value: 6.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  38 QELITLLNGALATELVCIARYKRHYYTVSGrdngtikAEFL-------EHAQQEQEHADWLAERIVQLNGKPDFNPATLL 110
Cdd:NF041388   22 EQIVDALNTDLAATYVLYHQLKKHHWNVEG-------AEFRdlhlflgEAAEDAEEAADELAERAQALGGVPVSGPAALE 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1922990879 111 ARSHAEY--DDSEDVQSMVRANLIAERVAIESYRQMI---VKIGdkDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:NF041388   95 EHAPVEPegEDVYDIRTSLENDLEMYGDIIESVRDHIelaENLG--DHATAELLREQLVELEEDAHHIEHYLE 165
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 34-171 1.00e-07

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: 49.04  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  34 QGDrQELITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDF-NPATLLAr 112
Cdd:TIGR00754   2 KGD-PDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRI- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879 113 shaeyddSEDVQSMVRANLIAERVAIESYRQMIVKIGDK-DPTTRHLLIKIMAVEEEHAD 171
Cdd:TIGR00754  80 -------GETVREMLEADLALELDVLNRLKEAIAYAEEVrDYVSRDLLEEILEDEEEHID 132
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 35-169 4.45e-07

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 47.79  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  35 GDRQELITLLNGALATELVCIarykrHYYTV-----SGRDNGTIKaEFLEHAQQE-QEHADWLAERIVQLNGK-----PD 103
Cdd:PRK13456   16 VDVDKLVELLVKNAAAEFTTY-----YYYTIlrahlIGLEGEGLK-EIAEDARLEdRNHFEALVPRIYELGGKlprdiRE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922990879 104 FnpATLLARSHAEY-DDSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEH 169
Cdd:PRK13456   90 F--HDISACPDAYLpENPTDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTYDLALAILQEEIEH 154
 
Name Accession Description Interval E-value
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 36-178 4.20e-30

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 107.68  E-value: 4.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  36 DRQELITLLNGALATELVCIarykrHYYT-----VSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLL 110
Cdd:COG2406    13 DVDELIELLNKAYADEWLAY-----YYYWigaknVKGLMGEGIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 111 ARSHAEYD---DSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:COG2406    88 ELSGCGYDlpeDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLG 158
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
36-178 5.21e-30

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 107.20  E-value: 5.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  36 DRQELITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPatllarsHA 115
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLQD-------LG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1922990879 116 EYDDSEDVQSMVRANLIAERVAIESYRQMIVKIGD-KDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:COG2193    74 KLRIGEDVEEMLECDLALELEAIALYREAIALCEEvGDYVSRDLLEEILEDEEEHIDWLETQLE 137
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 43-177 3.10e-25

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: 94.49  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  43 LLNGALATELVCIARYKRHYYTVSGRDngtIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLArSHAEYDDSED 122
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAPDPD---LKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLA-AYALPKTSDD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1922990879 123 VQSMVRANLIAERVAIESYRQMIVKIGdkDPTTRHLLIKIMAVEEEHADDMRDLM 177
Cdd:cd00657    78 PAEALRAALEVEARAIAAYRELIEQAD--DPELRRLLERILADEQRHAAWFRKLL 130
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 34-176 4.15e-25

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: 94.66  E-value: 4.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  34 QGDRQELITLLNGALATELvcIARYkrhYYT-----VSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPAT 108
Cdd:cd01052     1 GLDVDELIELLNKAFADEW--LAYY---YYTilakhVKGPEGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKD 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1922990879 109 LLARSHAEYD----DSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEHADDMRDL 176
Cdd:cd01052    76 WYEISGCKCGylppDPPDVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYDLALAILNEEIEHEEDLEEL 147
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 41-178 1.10e-19

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: 80.41  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  41 ITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLArsHAEYDDS 120
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLA--IEAPPSF 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1922990879 121 EDVQSMVRANLIAERVAIESYRQMI-VKIGDKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:pfam00210  79 GSVLEVLEAALEHEKKVTKSLRELIeLAEEEGDYATADFLQWFLDEQEEHEWFLEALLE 137
Dps COG0783
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ...
 36-170 7.06e-15

DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms];


Pssm-ID: 440546 [Multi-domain]  Cd Length: 156  Bit Score: 67.94  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  36 DRQELITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLARSH- 114
Cdd:COG0783    10 AREKVAEALNQLLADLYVLYLKTKNAHWNVKGPNFFSLHELFEELYDELREAIDEIAERIRALGGVPPGTLAEFAKLSTi 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1922990879 115 AEYD-DSEDVQSMVRANLIAERVAIESYRQMIVKIGD-KDPTTRHLLIKIMAVEEEHA 170
Cdd:COG0783    90 KEEPeGVVDAREMVEALLEDYEALIKTLREAIELADEaGDEGTADLLTDILRELEKRA 147
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
39-178 1.47e-13

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 64.36  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  39 ELITLLNGALATELVCIARYKRHYYTVSgrdNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATL----LARSH 114
Cdd:COG1633     1 SLLEILKEAIAMEEEAIEFYLELAEKAK---DPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEEsqpgLAELM 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1922990879 115 AEYDDSEDVQSMVRANLIAERVAIESYRQMIVKIgdKDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:COG1633    78 DKLDGSVSDAEALELAIATEKDAIEFYRELAAKV--GDPEIKKLFEELAADEKEHAALLEGLYD 139
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 34-171 1.05e-11

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: 59.48  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  34 QGDrQELITLLNGALATELVCIARYKRHYYTVsgRDNGTIK-AEFLEH-AQQEQEHADWLAERIVQLNGKPDFNPATLLA 111
Cdd:cd00907     1 KGD-PKVIEALNKALTGELTAINQYFLHARML--EDWGLEKlAERFRKeSIEEMKHADKLIERILFLEGLPNLQRLGKLR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1922990879 112 RshaeyddSEDVQSMVRANLIAERVAIESYRQMIV---KIGDKdpTTRHLLIKIMAVEEEHAD 171
Cdd:cd00907    78 I-------GEDVPEMLENDLALEYEAIAALNEAIAlceEVGDY--VSRDLLEEILEDEEEHID 131
DPS cd01043
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ...
 43-170 6.22e-10

DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.


Pssm-ID: 153102  Cd Length: 139  Bit Score: 54.47  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  43 LLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATLLARSH-AEYDDSE 121
Cdd:cd01043     2 ALNQLLADLYVLYLKLKNYHWNVKGPNFFALHELFEELYDELREAIDEIAERIRALGGKPLGTLKEYAELSTiKEEPAGV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 122 -DVQSMVRANLIAERVAIESYRQMIVKIGDK-DPTTRHLLIKIMAVEEEHA 170
Cdd:cd01043    82 lSAKEMVAELLEDYETLIEELREAIELADEAgDPATADLLTEIIRELEKQA 132
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
38-178 6.55e-10

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 55.34  E-value: 6.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  38 QELITLLNGALATELVCIARYKRHYYTVSGrdngtikAEFL-------EHAQQEQEHADWLAERIVQLNGKPDFNPATLL 110
Cdd:NF041388   22 EQIVDALNTDLAATYVLYHQLKKHHWNVEG-------AEFRdlhlflgEAAEDAEEAADELAERAQALGGVPVSGPAALE 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1922990879 111 ARSHAEY--DDSEDVQSMVRANLIAERVAIESYRQMI---VKIGdkDPTTRHLLIKIMAVEEEHADDMRDLME 178
Cdd:NF041388   95 EHAPVEPegEDVYDIRTSLENDLEMYGDIIESVRDHIelaENLG--DHATAELLREQLVELEEDAHHIEHYLE 165
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 34-171 1.00e-07

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: 49.04  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  34 QGDrQELITLLNGALATELVCIARYKRHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDF-NPATLLAr 112
Cdd:TIGR00754   2 KGD-PDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLqDLGKLRI- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879 113 shaeyddSEDVQSMVRANLIAERVAIESYRQMIVKIGDK-DPTTRHLLIKIMAVEEEHAD 171
Cdd:TIGR00754  80 -------GETVREMLEADLALELDVLNRLKEAIAYAEEVrDYVSRDLLEEILEDEEEHID 132
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 35-169 4.45e-07

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 47.79  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  35 GDRQELITLLNGALATELVCIarykrHYYTV-----SGRDNGTIKaEFLEHAQQE-QEHADWLAERIVQLNGK-----PD 103
Cdd:PRK13456   16 VDVDKLVELLVKNAAAEFTTY-----YYYTIlrahlIGLEGEGLK-EIAEDARLEdRNHFEALVPRIYELGGKlprdiRE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1922990879 104 FnpATLLARSHAEY-DDSEDVQSMVRANLIAERVAIESYRQMIVKIGDKDPTTRHLLIKIMAVEEEH 169
Cdd:PRK13456   90 F--HDISACPDAYLpENPTDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTYDLALAILQEEIEH 154
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 46-170 1.96e-06

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: 45.35  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  46 GALATELVCIARYKRHYYtVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDF---NPATLLARSHAEYDDSED 122
Cdd:cd07908    23 AGTNSELTAISQYIYQHL-ISEEKYPEIAETFLGIAIVEMHHLEILGQLIVLLGGDPRYrssSSDKFTYWTGKYVNYGES 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1922990879 123 VQSMVRANLIAERVAIESYRQMIVKIgdKDPTTRHLLIKIMAVEEEHA 170
Cdd:cd07908   102 IKEMLKLDIASEKAAIAKYKRQAETI--KDPYIRALLNRIILDEKLHI 147
PRK10635 PRK10635
bacterioferritin; Provisional
 34-171 5.76e-06

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 44.05  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  34 QGDRQeLITLLNGALATELVCIARYKRHYYTVsgRDNGTIKAEFLEHAQQ--EQEHADWLAERIVQLNGKPDFNPATLLa 111
Cdd:PRK10635    2 KGDVK-IINYLNKLLGNELVAINQYFLHARMF--KNWGLMRLNDVEYHESidEMKHADKYIERILFLEGIPNLQDLGKL- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 112 rshaeyDDSEDVQSMVRANLIAERVAIESYRQMIVKIGD-KDPTTRHLLIKIMAVEEEHAD 171
Cdd:PRK10635   78 ------NIGEDVEEMLRSDLRLELEGAKDLREAIAYADSvHDYVSRDMMIEILADEEGHID 132
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 43-177 5.97e-05

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 40.80  E-value: 5.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  43 LLNGALATELVCIARYKrHYYTVSGRDNGTIKAEFLEHAQQEQEHADWLAERIVQLNGKPDFNPATL----LARSHAEYD 118
Cdd:pfam02915   2 NLEKAIAGESSARRRYK-ELAEKAKNEYPQIAELFEEMAEEERRHAGFLNKLLKDLFPGLELIPLEHvrgyAEFPPKFLT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1922990879 119 DSEDVQSMVRanlIAERVAIESYRQMiVKIGDK--DPTTRHLLIKIMAVEEEHADDMRDLM 177
Cdd:pfam02915  81 TATNLEEAIE---GEYAEEEEMYRFY-EELAEKegYPEARKLFEDLAEAEKRHEERFRKLL 137
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 73-177 8.50e-05

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: 40.41  E-value: 8.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1922990879  73 IKAEFLEHAQQEQEHADWLAERIVQLNGK-----PDFNPATLLARSHAEYDDSEDVQSMVRANLIA---ERVAIESYRQM 144
Cdd:cd01045    29 LKKLFEELAEEEKEHAERLEELYEKLFGEelpelEPEDYKEEVEEEPEFKKALESLMDPLEALRLAieiEKDAIEFYEEL 108

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1922990879 145 IVKIgdKDPTTRHLLIKIMAVEEEHADDMRDLM 177
Cdd:cd01045   109 AEKA--EDPEVKKLFEELAEEERGHLRLLEELY 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH