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Conserved domains on  [gi|937514309|gb|ALI34796|]
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Ferritin-like domain protein [Candidatus Nitrosocosmicus oleophilus]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 1-160 2.63e-56

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


:

Pssm-ID: 441962  Cd Length: 165  Bit Score: 173.93  E-value: 2.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   1 MGKMSKEI-AGPGVEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQPT 78
Cdd:COG2406    1 MGKVGREIlVGVDVDELIELLNKAYADEWLAYYYYWIGAKNVKGLmGEGIKEELEDHAEEELNHAELLAERIYELGGTPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  79 DEPSQWEQDSGLGKLQPSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDHATYHLALELLDAELEDEQNIEDILAKL 158
Cdd:COG2406   81 LDPEEWAELSGCGYDLPEDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGDL 160


                 ..
gi 937514309 159 EI 160
Cdd:COG2406  161 ES 162
 
Name Accession Description Interval E-value
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 1-160 2.63e-56

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 173.93  E-value: 2.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   1 MGKMSKEI-AGPGVEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQPT 78
Cdd:COG2406    1 MGKVGREIlVGVDVDELIELLNKAYADEWLAYYYYWIGAKNVKGLmGEGIKEELEDHAEEELNHAELLAERIYELGGTPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  79 DEPSQWEQDSGLGKLQPSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDHATYHLALELLDAELEDEQNIEDILAKL 158
Cdd:COG2406   81 LDPEEWAELSGCGYDLPEDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGDL 160


                 ..
gi 937514309 159 EI 160
Cdd:COG2406  161 ES 162
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 13-135 1.14e-20

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: 82.34  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  13 VEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQPTDEPSQWEQDSGL- 90
Cdd:cd01052    4 VDELIELLNKAFADEWLAYYYYTILAKHVKGPeGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEISGCk 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 937514309  91 -GKLQPSRYlTLRSALEKALEFERAVIKHYNDLANNVKDKDHATYH 135
Cdd:cd01052   84 cGYLPPDPP-DVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYD 128
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 17-135 6.18e-11

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: 56.91  E-value: 6.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   17 VQMLKKAYGAELSAFHYFWFVSQNIEGLG--VLHQgFFEDRAKEELGHAKKVAFRLMQLETQPTDEPSQWEQDSGlgklq 94
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGfeGLHE-FFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEA----- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 937514309   95 PSRYLTLRSALEKALEFERAVIKHYNDLANNVKD-KDHATYH 135
Cdd:pfam00210  75 PPSFGSVLEVLEAALEHEKKVTKSLRELIELAEEeGDYATAD 116
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 1-134 1.32e-07

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 48.56  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   1 MGKMSKEI---AGPGVEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQ 76
Cdd:PRK13456   3 MAVVGREVvekSGVDVDKLVELLVKNAAAEFTTYYYYTILRAHLIGLeGEGLKEIAEDARLEDRNHFEALVPRIYELGGK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937514309  77 PTDEPSQWEQDSGLGKLQ-PSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDHATY 134
Cdd:PRK13456  83 LPRDIREFHDISACPDAYlPENPTDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTY 141
 
Name Accession Description Interval E-value
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 1-160 2.63e-56

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 173.93  E-value: 2.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   1 MGKMSKEI-AGPGVEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQPT 78
Cdd:COG2406    1 MGKVGREIlVGVDVDELIELLNKAYADEWLAYYYYWIGAKNVKGLmGEGIKEELEDHAEEELNHAELLAERIYELGGTPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  79 DEPSQWEQDSGLGKLQPSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDHATYHLALELLDAELEDEQNIEDILAKL 158
Cdd:COG2406   81 LDPEEWAELSGCGYDLPEDPTDVRAILEQNLKAERCAIKVYNELCNMTKGKDPVTYDLALDILEEEVEHEQDLEDLLGDL 160


                 ..
gi 937514309 159 EI 160
Cdd:COG2406  161 ES 162
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 13-135 1.14e-20

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: 82.34  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  13 VEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQPTDEPSQWEQDSGL- 90
Cdd:cd01052    4 VDELIELLNKAFADEWLAYYYYTILAKHVKGPeGEGIKEELEEAAEEELNHAELLAERIYELGGTPPRDPKDWYEISGCk 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 937514309  91 -GKLQPSRYlTLRSALEKALEFERAVIKHYNDLANNVKDKDHATYH 135
Cdd:cd01052   84 cGYLPPDPP-DVKGILKVNLKAERCAIKVYKELCDMTHGKDPVTYD 128
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 17-135 6.18e-11

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: 56.91  E-value: 6.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   17 VQMLKKAYGAELSAFHYFWFVSQNIEGLG--VLHQgFFEDRAKEELGHAKKVAFRLMQLETQPTDEPSQWEQDSGlgklq 94
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGfeGLHE-FFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEA----- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 937514309   95 PSRYLTLRSALEKALEFERAVIKHYNDLANNVKD-KDHATYH 135
Cdd:pfam00210  75 PPSFGSVLEVLEAALEHEKKVTKSLRELIELAEEeGDYATAD 116
PRK13456 PRK13456
DNA protection protein DPS; Provisional
 1-134 1.32e-07

DNA protection protein DPS; Provisional


Pssm-ID: 237389  Cd Length: 186  Bit Score: 48.56  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309   1 MGKMSKEI---AGPGVEGTVQMLKKAYGAELSAFHYFWFVSQNIEGL-GVLHQGFFEDRAKEELGHAKKVAFRLMQLETQ 76
Cdd:PRK13456   3 MAVVGREVvekSGVDVDKLVELLVKNAAAEFTTYYYYTILRAHLIGLeGEGLKEIAEDARLEDRNHFEALVPRIYELGGK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937514309  77 PTDEPSQWEQDSGLGKLQ-PSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDHATY 134
Cdd:PRK13456  83 LPRDIREFHDISACPDAYlPENPTDPKEILKVLLEAERCAIRTYTEICDMTAGKDPRTY 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 19-134 1.07e-06

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: 45.18  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  19 MLKKAYGAELSAFHYFWFVSQNIEGLGVlhQGFFEDRAKEELGHAKKVAFRLMQLETQPTDEPSQweqdSGLGKLQPSRY 98
Cdd:cd00657    2 LLNDALAGEYAAIIAYGQLAARAPDPDL--KDELLEIADEERRHADALAERLRELGGTPPLPPAH----LLAAYALPKTS 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 937514309  99 LTLRSALEKALEFERAVIKHYNDLANNVKDKDHATY 134
Cdd:cd00657   76 DDPAEALRAALEVEARAIAAYRELIEQADDPELRRL 111
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
12-128 3.24e-06

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 44.41  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  12 GVEGTVQMLKKAYGAELSAF-----HYFWFVSQNIEGLGvlhqGFFEDRAKEELGHAKKVAFRLMQLETQPTDEPsqweq 86
Cdd:COG2193    1 GDPKVIELLNKALANELTAInqyflHARMLKNWGLEKLA----EKFYEESIEEMKHADKLIERILFLGGLPNLQD----- 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 937514309  87 dsgLGKLQPSRylTLRSALEKALEFERAVIKHYND---LANNVKD 128
Cdd:COG2193   72 ---LGKLRIGE--DVEEMLECDLALELEAIALYREaiaLCEEVGD 111
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
17-131 7.24e-06

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 43.17  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  17 VQMLKKAYGAELSAFHYFWFVSQNIEGLGVlhQGFFEDRAKEELGHAKKVAFRLMQLETQPTDEPsQWEQDSGLGKLQP- 95
Cdd:COG1633    3 LEILKEAIAMEEEAIEFYLELAEKAKDPEL--KKLFEELAEEEKKHAELLEKLYEKLGGKPVAPP-EEESQPGLAELMDk 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937514309  96 -SRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDH 131
Cdd:COG1633   80 lDGSVSDAEALELAIATEKDAIEFYRELAAKVGDPEI 116
FtnA COG1528
Ferritin [Inorganic ion transport and metabolism];
14-134 4.98e-05

Ferritin [Inorganic ion transport and metabolism];


Pssm-ID: 441137  Cd Length: 158  Bit Score: 41.27  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  14 EGTVQMLKKAYGAEL-SAFHYF----WFVSQNIEGLGvlhqGFFEDRAKEELGHAKKVaFRLMQ-----LETQPTDEPsq 83
Cdd:COG1528    4 EKMEKALNEQINLEFySSYLYLamaaWCDEKGLPGFA----NFFRVQAQEERTHAMKF-FDYLNdrggrVELPAIDAP-- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 937514309  84 weqdsglgklqPSRYLTLRSALEKALEFERAVIKHYNDLANN-VKDKDHATY 134
Cdd:COG1528   77 -----------PNEFESLLEVFEAALEHEQKVTKSINELVDLaREEKDYATE 117
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 16-128 1.44e-04

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: 39.84  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  16 TVQMLKKAYGAELSAFH-YF--------WfvsqnieGLGVLHQgFFEDRAKEELGHAKKVAFRLMQLEtqptdepsqweq 86
Cdd:cd00907    6 VIEALNKALTGELTAINqYFlharmledW-------GLEKLAE-RFRKESIEEMKHADKLIERILFLE------------ 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 937514309  87 dsGLGKLQPSRYL----TLRSALEKALEFERAVIKHYND---LANNVKD 128
Cdd:cd00907   66 --GLPNLQRLGKLrigeDVPEMLENDLALEYEAIAALNEaiaLCEEVGD 112
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 20-131 2.05e-04

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: 39.25  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  20 LKKAYGAELSAFHYFWFVSQNIEGLGVlhQGFFEDRAKEELGHAKKVA--FRLMQLETQPTDEPSQW---EQDSGLGKLQ 94
Cdd:cd01045    3 LALAIKMEEEAAEFYLELAEKAKDPEL--KKLFEELAEEEKEHAERLEelYEKLFGEELPELEPEDYkeeVEEEPEFKKA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937514309  95 PSRYLTLRSALEKALEFERAVIKHYNDLANNVKDKDH 131
Cdd:cd01045   81 LESLMDPLEALRLAIEIEKDAIEFYEELAEKAEDPEV 117
Nonheme_Ferritin cd01055
nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a ...
 14-160 2.72e-03

nonheme-containing ferritins; Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite.


Pssm-ID: 153113  Cd Length: 156  Bit Score: 36.31  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937514309  14 EGTVQMLKKAYGAEL-SAFHYF----WFVSQNIEGLGvlhqGFFEDRAKEELGHAKKVAFRLMQ----LETQPTDEPsqw 84
Cdd:cd01055    2 EKLEKALNEQINLELySSYLYLamaaWFDSKGLDGFA----NFFRVQAQEEREHAMKFFDYLNDrggrVELPAIEAP--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937514309  85 eqdsglgklqPSRYLTLRSALEKALEFERAVIKHYNDLANN-VKDKDHATYHLALELLDAELEDEQNIEDILAKLEI 160
Cdd:cd01055   75 ----------PSEFESLLEVFEAALEHEQKVTESINNLVDLaLEEKDYATFNFLQWFVKEQVEEEALARDILDKLKL 141
 
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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