Summary: Cytochrome B6-F complex subunit VI (PetL)
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Cytochrome B6-F complex subunit VI (PetL) Provide feedback
This family consists of several Cytochrome B6-F complex subunit VI (PetL) proteins found in several plant species. PetL is one of the small subunits which make up The cytochrome b(6)f complex. PetL is strictly required neither for the accumulation nor for the function of cytochrome b6f; in its absence, however, the complex becomes unstable in vivo in aging cells and labile in vitro. It has been suggested that the N-terminus of the protein is likely to lie in the thylakoid lumen .
Zito F, Vinh J, Popot JL, Finazzi G; , J Biol Chem 2002;277:12446-12455.: Chimeric fusions of subunit IV and PetL in the b6f complex of Chlamydomonas reinhardtii: structural implications and consequences on state transitions. PUBMED:11796719 EPMC:11796719
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007802This family consists of several Cytochrome B6-F complex subunit VI (PetL) proteins found in a number of plant species. PetL is one of the small subunits which make up the cytochrome b(6)f complex. PetL is not absolutely required for either the accumulation or for the function of cytochrome b6f; in its absence, however, the complex becomes unstable in vivo in aging cells and labile in vitro. It has been suggested that the N terminus of the protein is likely to lie in the thylakoid lumen [PUBMED:11796719].
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|Cellular component||cytochrome b6f complex (GO:0009512)|
|Molecular function||electron carrier activity (GO:0009055)|
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Curation and family details
|Seed source:||Pfam-B_6510 (release 7.7)|
|Number in seed:||28|
|Number in full:||723|
|Average length of the domain:||30.30 aa|
|Average identity of full alignment:||69 %|
|Average coverage of the sequence by the domain:||83.62 %|
|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:||9|
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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 PetL domain has been found. There are 2 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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