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IPR002327 is a Cytochrome c, class IA/ IB.
<p>Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulfhydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of properties and function in a large number of different redox processes.</p> <p>Ambler [[cite:PUB00000610]] recognised four classes of cytC. Class I includes the low-spin soluble cytC of mitochondria and bacteria, with the haem-attachment site towards the N terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C terminus [[cite:PUB00095221]]. On the basis of sequence similarity, class I cytC were further subdivided into five classes, IA to IE. Class IB includes the eukaryotic mitochondrial cyt C and prokaryotic 'short' cyt C2 exemplified by Rhodopila globiformis cyt C2; Class IA includes 'long' cyt C2, such as Rhodospirillum rubrum cyt C2 and Aquaspirillum itersonii cyt C-550, which have several extra loops by comparison with Class IB cyt C.</p> <p>Class I cytC has a characterised fold which comprises 5 α-helices arranged in a unique tertiary structure and a conserved N-terminal sequence -Cys-Xxx-Xxx-Cys-His- where the cysteines mediate the covalent cross-linking of the heme to the protein and the His [[cite:PUB00095221]].The 3D structures of a considerable number of class IA and IB cytC have been determined. The proteins consist of 3-6 α-helices; the three most conserved 'core' helices form a 'basket' around the haem group, with one haem edge exposed to the solvent. Most class I cytC have conserved aromatic residues clustered around the haem and axial ligands.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Electron transfer activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. | ||
| Molecular function | Heme binding | Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: cytochrome c-like [Cucumis sativus] gi|449457373|ref|XP_004146423.1| | 9 | ||
| – | Cytochrome c [Medicago truncatula] gi|357481261|ref|XP_003610916.1| | 7 | ||
| – | Cytochrome c; TAIR: AT4G10040.1 cytochrome c-2; Swiss-Prot: sp|P00051|CYC_CUCMA Cytochrome c; TrEMBL-Plants: tr|I3T359|I3T359_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0489900 | 10 | ||
| – | Cytochrome c; TAIR: AT4G10040.1 cytochrome c-2; Swiss-Prot: sp|P00052|CYC_VIGRR Cytochrome c; TrEMBL-Plants: tr|I3SL85|I3SL85_LOTJA Uncharacterized protein; Found in the gene: LotjaGi2g1v0446000 | 10 | ||
| – | Cytochrome c; TAIR: AT4G10040.1 cytochrome c-2; Swiss-Prot: sp|P00051|CYC_CUCMA Cytochrome c; TrEMBL-Plants: tr|I3T359|I3T359_LOTJA Uncharacterized protein; Found in the gene: LotjaGi6g1v0216000 | 10 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF46626 | SUPERFAMILY | 1 | 20.00 |