Summary: Sirohaem biosynthesis protein C-terminal
Sirohaem biosynthesis protein C-terminal Provide feedback
This domain is the C-terminus of a multifunctional enzyme which catalyses the biosynthesis of sirohaem. Both of the catalytic activities of this enzyme (precorrin-2 dehydrogenase EC:188.8.131.52) and sirohydrochlorin ferrochelatase ( EC:184.108.40.206) are located in the N-terminal domain of this enzyme, PF13241 .
Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ;, EMBO J. 2002;21:2068-2075.: The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. PUBMED:11980703 EPMC:11980703
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This tab holds annotation information from the InterPro database.
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Curation and family details
This family is new in this Pfam release.
|Number in seed:||15|
|Number in full:||193|
|Average length of the domain:||66.60 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||18.74 %|
|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:||1|
|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 Sirohm_synth_C domain has been found. There are 3 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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