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Conserved domains on  [gi|851216343|ref|WP_048111754|]
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rubrerythrin [Candidatus Methanoplasma termitum]

Protein Classification

rubrerythrin family protein( domain architecture ID 11446349)

rubrerythrin family protein such as Clostridium acetobutylicum rubrerythrin-1 and -2, which function as the terminal components of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YotD COG1592
Rubrerythrin [Energy production and conversion];
1-176 1.10e-89

Rubrerythrin [Energy production and conversion];


:

Pssm-ID: 441200 [Multi-domain]  Cd Length: 180  Bit Score: 259.75  E-value: 1.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   1 MELKGSKTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLWFKALHGGCIPE----TVENLK 76
Cdd:COG1592    1 MSLKGTKTEKNLLAAFAGESQARNRYTAFAKKAKKEGYPQIARLFRATAEAEKEHAKNHFKLLKGAAGPVgigdTAENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343  77 DAASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIENGKVFKKDKVVVWKCQNCGYLHVGK 156
Cdd:COG1592   81 AAIEGETYEWTEMYPEFAKVAEEEGFKEAARSFRYAAEAEKIHAERYKKLLENLEAGKVFKKDEEVVWVCPVCGYIHEGK 160

                        170       180
                 ....*....|....*....|
gi 851216343 157 EAPAVCPTCNHPQSFFEVQS 176
Cdd:COG1592  161 EAPEKCPVCGHPKSYFELFA 180
 
Name Accession Description Interval E-value
YotD COG1592
Rubrerythrin [Energy production and conversion];
1-176 1.10e-89

Rubrerythrin [Energy production and conversion];


Pssm-ID: 441200 [Multi-domain]  Cd Length: 180  Bit Score: 259.75  E-value: 1.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   1 MELKGSKTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLWFKALHGGCIPE----TVENLK 76
Cdd:COG1592    1 MSLKGTKTEKNLLAAFAGESQARNRYTAFAKKAKKEGYPQIARLFRATAEAEKEHAKNHFKLLKGAAGPVgigdTAENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343  77 DAASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIENGKVFKKDKVVVWKCQNCGYLHVGK 156
Cdd:COG1592   81 AAIEGETYEWTEMYPEFAKVAEEEGFKEAARSFRYAAEAEKIHAERYKKLLENLEAGKVFKKDEEVVWVCPVCGYIHEGK 160

                        170       180
                 ....*....|....*....|
gi 851216343 157 EAPAVCPTCNHPQSFFEVQS 176
Cdd:COG1592  161 EAPEKCPVCGHPKSYFELFA 180
Rubrerythrin cd01041
Rubrerythrin, ferritin-like diiron-binding domain; Rubrerythrin domain is a nonheme iron ...
 7-131 2.80e-59

Rubrerythrin, ferritin-like diiron-binding domain; Rubrerythrin domain is a nonheme iron binding domain found in many air-sensitive bacteria and archaea and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The homodimeric rubrerythrin protein contains a binuclear metal center located within a four helix bundle. Many, but not all, rubrerythrin proteins have a second domain with a rubredoxin-like hexacoordinated iron center. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system but its function is still poorly understood.


Pssm-ID: 153100  Cd Length: 134  Bit Score: 181.24  E-value: 2.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   7 KTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLWFKALHGGCIPE---------TVENLKD 77
Cdd:cd01041    1 KTEKNLLAAFAGESQARNRYTYFAEKARKEGYEQIARLFRATAENEKEHAKGHFKLLKGLGGGDtgppigigdTLENLKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851216343  78 AASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIE 131
Cdd:cd01041   81 AIAGETYEYTEMYPEFAEVAEEEGFKEAARSFEAIAEAEKVHAERYKKALENLE 134
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 11-127 1.30e-20

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 82.79  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   11 NLMTAFAGESQARTKYTYYASQARKEgYNQVADIFMETAENEKEHAKL---WFKALHGGCIPE----------------- 70
Cdd:pfam02915   2 NLEKAIAGESSARRRYKELAEKAKNE-YPQIAELFEEMAEEERRHAGFlnkLLKDLFPGLELIplehvrgyaefppkflt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 851216343   71 TVENLKDAASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELL 127
Cdd:pfam02915  81 TATNLEEAIEGEYAEEEEMYRFYEELAEKEGYPEARKLFEDLAEAEKRHEERFRKLL 137
 
Name Accession Description Interval E-value
YotD COG1592
Rubrerythrin [Energy production and conversion];
1-176 1.10e-89

Rubrerythrin [Energy production and conversion];


Pssm-ID: 441200 [Multi-domain]  Cd Length: 180  Bit Score: 259.75  E-value: 1.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   1 MELKGSKTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLWFKALHGGCIPE----TVENLK 76
Cdd:COG1592    1 MSLKGTKTEKNLLAAFAGESQARNRYTAFAKKAKKEGYPQIARLFRATAEAEKEHAKNHFKLLKGAAGPVgigdTAENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343  77 DAASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIENGKVFKKDKVVVWKCQNCGYLHVGK 156
Cdd:COG1592   81 AAIEGETYEWTEMYPEFAKVAEEEGFKEAARSFRYAAEAEKIHAERYKKLLENLEAGKVFKKDEEVVWVCPVCGYIHEGK 160

                        170       180
                 ....*....|....*....|
gi 851216343 157 EAPAVCPTCNHPQSFFEVQS 176
Cdd:COG1592  161 EAPEKCPVCGHPKSYFELFA 180
Rubrerythrin cd01041
Rubrerythrin, ferritin-like diiron-binding domain; Rubrerythrin domain is a nonheme iron ...
 7-131 2.80e-59

Rubrerythrin, ferritin-like diiron-binding domain; Rubrerythrin domain is a nonheme iron binding domain found in many air-sensitive bacteria and archaea and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The homodimeric rubrerythrin protein contains a binuclear metal center located within a four helix bundle. Many, but not all, rubrerythrin proteins have a second domain with a rubredoxin-like hexacoordinated iron center. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system but its function is still poorly understood.


Pssm-ID: 153100  Cd Length: 134  Bit Score: 181.24  E-value: 2.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   7 KTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLWFKALHGGCIPE---------TVENLKD 77
Cdd:cd01041    1 KTEKNLLAAFAGESQARNRYTYFAEKARKEGYEQIARLFRATAENEKEHAKGHFKLLKGLGGGDtgppigigdTLENLKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851216343  78 AASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIE 131
Cdd:cd01041   81 AIAGETYEYTEMYPEFAEVAEEEGFKEAARSFEAIAEAEKVHAERYKKALENLE 134
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 11-127 1.30e-20

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 82.79  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   11 NLMTAFAGESQARTKYTYYASQARKEgYNQVADIFMETAENEKEHAKL---WFKALHGGCIPE----------------- 70
Cdd:pfam02915   2 NLEKAIAGESSARRRYKELAEKAKNE-YPQIAELFEEMAEEERRHAGFlnkLLKDLFPGLELIplehvrgyaefppkflt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 851216343   71 TVENLKDAASGENYEHTQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELL 127
Cdd:pfam02915  81 TATNLEEAIEGEYAEEEEMYRFYEELAEKEGYPEARKLFEDLAEAEKRHEERFRKLL 137
rubredoxin_SM cd00729
Rubredoxin, Small Modular nonheme iron binding domain containing a [Fe(SCys)4] center, present ...
 146-174 1.71e-10

Rubredoxin, Small Modular nonheme iron binding domain containing a [Fe(SCys)4] center, present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238371 [Multi-domain]  Cd Length: 34  Bit Score: 53.35  E-value: 1.71e-10
                         10        20
                 ....*....|....*....|....*....
gi 851216343 146 CQNCGYLHVGKEAPAVCPTCNHPQSFFEV 174
Cdd:cd00729    5 CPVCGYIHEGEEAPEKCPICGAPKEKFEE 33
Rubrerythrin_like cd01046
rubrerythrin-like, diiron-binding domain; Rubrerythrin-like domain, similar to rubrerythrin, a ...
 7-128 1.06e-09

rubrerythrin-like, diiron-binding domain; Rubrerythrin-like domain, similar to rubrerythrin, a nonheme iron binding domain found in many air-sensitive bacteria and archaea, and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system. The rubrerythrin protein has two domains, a binuclear metal center located within a four-helix bundle of the rubrerythrin domain, and a rubredoxin domain. The Rubrerythrin-like domains in this CD are singular domains (no C-terminus rubredoxin domain) and are phylogenetically distinct from rubrerythrin domains of rubrerythrin-rubredoxin proteins.


Pssm-ID: 153105  Cd Length: 123  Bit Score: 53.46  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343   7 KTEANLMTAFAGESQARTKYTYYASQARKEGYNQVADIFMETAENEKEHAKLwFKALHGGCIPETVENLKDAASGEnYEH 86
Cdd:cd01046    1 DLEEDLEANFKGETTEVGMYLAMARVAQREGYPEVAEELKRIAMEEAEHAAR-FAELLGKVSEDTKENLEMMLEGE-AGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 851216343  87 TQMYKDFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLK 128
Cdd:cd01046   79 NEGKKDAATEAKAEGLDEAHDFFHEAAKDEARHGKMLKGLLE 120
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 146-174 1.25e-08

Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238210 [Multi-domain]  Cd Length: 33  Bit Score: 48.32  E-value: 1.25e-08
                         10        20
                 ....*....|....*....|....*....
gi 851216343 146 CQNCGYLHVGKEAPAVCPTCNHPQSFFEV 174
Cdd:cd00350    4 CPVCGYIYDGEEAPWVCPVCGAPKDKFEK 32
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
12-132 1.73e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 37.01  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851216343  12 LMTAFAGESQARTKYTYYASQARKEgynQVADIFMETAENEKEHAKLWFKALHGGCIPETVENlkdaasgenyEHTQMYK 91
Cdd:COG1633    6 LKEAIAMEEEAIEFYLELAEKAKDP---ELKKLFEELAEEEKKHAELLEKLYEKLGGKPVAPP----------EEESQPG 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 851216343  92 DFEATARKEGFKQIADQFKLVGEIEAVHEKRYLELLKNIEN 132
Cdd:COG1633   73 LAELMDKLDGSVSDAEALELAIATEKDAIEFYRELAAKVGD 113
 
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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