Summary: Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain
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Thioredoxin fold Edit Wikipedia article
|One molecule of human thioredoxin (PDB ID 1ERT), a canonical example of the thioredoxin fold class.|
The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical example thioredoxin and is found in both prokaryotic and eukaryotic proteins. It is an example of an alpha/beta protein fold that has oxidoreductase activity. The fold's spatial topology consists of a four-stranded antiparallel beta sheet sandwiched between three alpha helices. The strand topology is 2134 with 3 antiparallel to the rest.
 Sequence conservation
Despite sequence variability in many regions of the fold, thioredoxin proteins share a common active site sequence with two reactive cysteine residues: Cys-X-Y-Cys, where X and Y are often but not necessarily hydrophobic amino acids. The reduced form of the protein contains two free thiol groups at the cysteine residues, whereas the oxidized form contains a disulfide bond between them.
 Disulfide bond formation
Different thioredoxin fold-containing proteins vary greatly in their reactivity and in the pKa of their free thiols, which derives from the ability of the overall protein structure to stabilize the activated thiolate. Although the structure is fairly consistent among proteins containing the thioredoxin fold, the pKa is extremely sensitive to small variations in structure, especially in the placement of protein backbone atoms near the first cysteine.
Human proteins containing this domain include:
- P4HB; P5; PDIA2; PDIA3; PDIA4; PDIA5; PDIA6; PDILT
- QSOX1; QSOX2
- TXN; TXN2; TXNDC1; TXNDC10; TXNDC11; TXNDC13; TXNDC14; TXNDC15; TXNDC16; TXNDC2; TXNDC3; TXNDC4; TXNDC5; TXNDC6; TXNDC8; TXNL1; TXNL3
- Creighton TE. (2000). Protein folding coupled to disulphide-bond formation. In Mechanisms of Protein Folding 2nd ed. Editor RH Pain. Oxford University Press.
Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain Provide feedback
The proteins in this family are located in the mitochondrion. The family includes ribosomal protein L51, and S25. This family also includes mitochondrial NADH-ubiquinone oxidoreductase B8 subunit (CI-B8) EC:188.8.131.52. It is not known whether all members of this family form part of the NADH-ubiquinone oxidoreductase and whether they are also all ribosomal proteins.
Gan X, Kitakawa M, Yoshino KI, Oshiro N, Yonezawa K, Isono K; , Eur J Biochem 2002;269:5203-5214.: Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components. PUBMED:12392552 EPMC:12392552
Koc EC, Burkhart W, Blackburn K, Moseley A, Koc H, Spremulli LL; , J Biol Chem 2000;275:32585-32591.: A proteomics approach to the identification of mammalian mitochondrial small subunit ribosomal proteins. PUBMED:10938081 EPMC:10938081
Ton C, Hwang DM, Dempsey AA, Liew CC; , Biochem Biophys Res Commun 1997;241:589-594.: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. PUBMED:9425316 EPMC:9425316
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007741Proteins containing this domain are located in the mitochondrion and include ribosomal protein L51, and S25. This domain is also found in mitochondrial NADH-ubiquinone oxidoreductase B8 subunit (CI-B8) EC. It is not known whether all members of this family form part of the NADH-ubiquinone oxidoreductase and whether they are also all ribosomal proteins.
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Curation and family details
|Seed source:||Pfam-B_9461 (release 7.6)|
|Author:||Wood V, Bateman A, Finn RD|
|Number in seed:||67|
|Number in full:||788|
|Average length of the domain:||54.90 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||38.29 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the L51_S25_CI-B8 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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