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Conserved domains on  [gi|489610388|ref|WP_003514829|]
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PA2169 family four-helix-bundle protein [Acetivibrio thermocellus]

Protein Classification

ferritin-like domain-containing protein( domain architecture ID 10560096)

ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; similar to Pseudomonas aeruginosa PA2169

CATH:  1.20.1260.10
Gene Ontology:  GO:0046872
PubMed:  8749363|9444766|3304136
SCOP:  4004279

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF2383 pfam09537
Domain of unknown function (DUF2383); Members of this protein family are found mostly in the ...
 12-114 2.32e-31

Domain of unknown function (DUF2383); Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


:

Pssm-ID: 430673  Cd Length: 106  Bit Score: 108.07  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388   12 LNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKFKG--TSD 89
Cdd:pfam09537   2 LNDLIETLYDGEDGYKTAAENVKDPQLKTLLQRRAAERRAAARELQSEIRALGGEPEDGGSFAGTLHRAWVDLKSalTSN 81

                          90       100
                  ....*....|....*....|....*
gi 489610388   90 DTEFILKDAAESENKGIKMAEELVR 114
Cdd:pfam09537  82 DEEAILEELERGEDAALEAYEEALE 106
 
Name Accession Description Interval E-value
DUF2383 pfam09537
Domain of unknown function (DUF2383); Members of this protein family are found mostly in the ...
 12-114 2.32e-31

Domain of unknown function (DUF2383); Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


Pssm-ID: 430673  Cd Length: 106  Bit Score: 108.07  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388   12 LNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKFKG--TSD 89
Cdd:pfam09537   2 LNDLIETLYDGEDGYKTAAENVKDPQLKTLLQRRAAERRAAARELQSEIRALGGEPEDGGSFAGTLHRAWVDLKSalTSN 81

                          90       100
                  ....*....|....*....|....*
gi 489610388   90 DTEFILKDAAESENKGIKMAEELVR 114
Cdd:pfam09537  82 DEEAILEELERGEDAALEAYEEALE 106
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 12-143 2.28e-24

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: 91.02  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388  12 LNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMnkfkGTSDDT 91
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALP----KTSDDP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489610388  92 EFILKDAAESENKGIKMAEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLL 143
Cdd:cd00657   79 AEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
22-144 4.90e-12

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 59.35  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388  22 AIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMG--SMAEVMNKFKGTSDDTEfILKDAA 99
Cdd:COG1633   16 AIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESqpGLAELMDKLDGSVSDAE-ALELAI 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489610388 100 ESENKGIKMAEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLLQ 144
Cdd:COG1633   95 ATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYD 139
TIGR02284 TIGR02284
conserved hypothetical protein; Members of this protein family are found mostly in the ...
 8-142 2.15e-06

conserved hypothetical protein; Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


Pssm-ID: 131337  Cd Length: 139  Bit Score: 44.44  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388    8 VIEELNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKFKG- 86
Cdd:TIGR02284   1 TIHSLNDLIEISIDGKDGFEESAEEVKDPELATLFRRIAGEKSAIVSELQQVVASLGGKPEDHGSMVGSLHQFWGKIRAt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489610388   87 -TSDDTEFILKDAAESENKGIKMAEE-LVRGDLDDESRKVVEKILDVNRKHVSQLNNL 142
Cdd:TIGR02284  81 lTPNDDYVVLEEAERGEDRAKKAYDEtLADQDTPAAARDVALRQYPGVRACHDVIRAL 138
 
Name Accession Description Interval E-value
DUF2383 pfam09537
Domain of unknown function (DUF2383); Members of this protein family are found mostly in the ...
 12-114 2.32e-31

Domain of unknown function (DUF2383); Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


Pssm-ID: 430673  Cd Length: 106  Bit Score: 108.07  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388   12 LNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKFKG--TSD 89
Cdd:pfam09537   2 LNDLIETLYDGEDGYKTAAENVKDPQLKTLLQRRAAERRAAARELQSEIRALGGEPEDGGSFAGTLHRAWVDLKSalTSN 81

                          90       100
                  ....*....|....*....|....*
gi 489610388   90 DTEFILKDAAESENKGIKMAEELVR 114
Cdd:pfam09537  82 DEEAILEELERGEDAALEAYEEALE 106
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 12-143 2.28e-24

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: 91.02  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388  12 LNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMnkfkGTSDDT 91
Cdd:cd00657    3 LNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALP----KTSDDP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489610388  92 EFILKDAAESENKGIKMAEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLL 143
Cdd:cd00657   79 AEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
22-144 4.90e-12

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 59.35  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388  22 AIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMG--SMAEVMNKFKGTSDDTEfILKDAA 99
Cdd:COG1633   16 AIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPPEEESqpGLAELMDKLDGSVSDAE-ALELAI 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489610388 100 ESENKGIKMAEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLLQ 144
Cdd:COG1633   95 ATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYD 139
TIGR02284 TIGR02284
conserved hypothetical protein; Members of this protein family are found mostly in the ...
 8-142 2.15e-06

conserved hypothetical protein; Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.


Pssm-ID: 131337  Cd Length: 139  Bit Score: 44.44  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388    8 VIEELNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKFKG- 86
Cdd:TIGR02284   1 TIHSLNDLIEISIDGKDGFEESAEEVKDPELATLFRRIAGEKSAIVSELQQVVASLGGKPEDHGSMVGSLHQFWGKIRAt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489610388   87 -TSDDTEFILKDAAESENKGIKMAEE-LVRGDLDDESRKVVEKILDVNRKHVSQLNNL 142
Cdd:TIGR02284  81 lTPNDDYVVLEEAERGEDRAKKAYDEtLADQDTPAAARDVALRQYPGVRACHDVIRAL 138
Ferritin_like_AB cd01045
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 26-143 1.06e-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: 39.64  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388  26 YERYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVPVDGP------GFMGSMAEVMNKFKGTSDDTEfILKDAA 99
Cdd:cd01045   17 YLELAEKAKDPELKKLFEELAEEEKEHAERLEELYEKLFGEELPELepedykEEVEEEPEFKKALESLMDPLE-ALRLAI 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489610388 100 ESENKGIKMAEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLL 143
Cdd:cd01045   96 EIEKDAIEFYEELAEKAEDPEVKKLFEELAEEERGHLRLLEELY 139
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
5-143 3.57e-04

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


Pssm-ID: 441796  Cd Length: 152  Bit Score: 38.25  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388   5 DNVVIEELNSLLEGNYMAIHGYERYIQHVKDPNIKK---ELQRIQQEHKQNSALIAERIQNLGGVPVdgpgfMGSMAEVM 81
Cdd:COG2193    2 DPKVIELLNKALANELTAINQYFLHARMLKNWGLEKlaeKFYEESIEEMKHADKLIERILFLGGLPN-----LQDLGKLR 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489610388  82 nkfkgTSDDTEFILKDAAESENKGIKM---AEELVRGDLDDESRKVVEKILDVNRKHVSQLNNLL 143
Cdd:COG2193   77 -----IGEDVEEMLECDLALELEAIALyreAIALCEEVGDYVSRDLLEEILEDEEEHIDWLETQL 136
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 1-45 2.97e-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: 35.72  E-value: 2.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489610388   1 MNNKDNVVIEELNSLLEGNYMAIHGYERYIQHVKDPNIKKELQRI 45
Cdd:cd07908   95 YVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRI 139
DPS COG2406
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ...
 8-113 7.78e-03

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


Pssm-ID: 441962  Cd Length: 165  Bit Score: 34.88  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388   8 VIEELNSLLEGNYMAIHGYERYIQHVKDPN---IKKELQRIQQEHKQNSALIAERIQNLGGVPVDGPGFMGSMAEVMNKF 84
Cdd:COG2406   17 LIELLNKAYADEWLAYYYYWIGAKNVKGLMgegIKEELEDHAEEELNHAELLAERIYELGGTPPLDPEEWAELSGCGYDL 96

                         90       100
                 ....*....|....*....|....*....
gi 489610388  85 KGTSDDTEFILKDAAESENKGIKMAEELV 113
Cdd:COG2406   97 PEDPTDVRAILEQNLKAERCAIKVYNELC 125
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 9-144 8.51e-03

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: 34.57  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489610388    9 IEELNSLLEG------NYMAIHgyeRYIQHVKDPNIKKELQRIQQEHKQNSALIAERIQNLGGVP---------VDGPGF 73
Cdd:pfam00210   1 IAALNEQLADeltasyQYLQMH---WYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPngtrvellaIEAPPS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489610388   74 MGSMAEVMnkfkgtsddtEFILKD---AAESENKGIKMAEELVrgdlDDESRKVVEKILDVNRKHVSQLNNLLQ 144
Cdd:pfam00210  78 FGSVLEVL----------EAALEHekkVTKSLRELIELAEEEG----DYATADFLQWFLDEQEEHEWFLEALLE 137
 
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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