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Annotation rule MF_00610 |
General rule information
[?]
Accession |
MF_00610 |
Dates |
23-DEC-2002 (Created) 19-JAN-2021 (Last updated, Version 48) |
Scope |
Bacteria; Cyanobacteria
Plastid |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Cytochrome f;
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Flags:
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Precursor;
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Function |
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. |
Cofactor |
heme Note: Binds 1 heme group covalently. |
Subunit |
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer. |
case <OG:Chloroplast>
Subcellular location |
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. |
else case <OC:Gloeobacter>
Subcellular location |
Cell inner membrane; Single-pass membrane protein. |
else
Subcellular location |
Cellular thylakoid membrane; Single-pass membrane protein. |
end case
Similarity |
Belongs to the cytochrome f family. |
case <OC:Gloeobacter>
else
end case
GO:0009055; Molecular function: electron transfer activity.
GO:0015979; Biological process: photosynthesis.
case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else case <OC:Gloeobacter>
else
GO:0042651; Cellular component: thylakoid membrane.
end case
General |
Signal; -; 1; trigger=yes; |
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Transmembrane; -; 1; trigger=yes; |
From: CYF_BRARR (P36438) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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METAL
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36
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36
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Iron (heme axial ligand); via amino nitrogen
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[FY]
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METAL
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60
|
|
60
|
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Iron (heme axial ligand)
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|
|
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H
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|
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BINDING
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56
|
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56
|
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Heme; covalent
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C
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BINDING
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59
|
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59
|
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Heme; covalent
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C
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Additional information
[?]
Size range |
300-342 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
In LEPTE the N-terminus is unusually long, not used in seed alignment or size range. In GLOVI the first conserved heme axial ligand Phe or Tyr is a Trp, the sequence is designated atypical. |