Summary: Lanthionine synthetase C-like protein
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Lanthionine synthetase C-like protein Provide feedback
Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs . Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains . This region contains seven internal repeats.
Mayer H, Bauer H, Breuss J, Ziegler S, Prohaska R; , Gene 2001;269:73-80.: Characterization of rat LANCL1, a novel member of the lanthionine synthetase C-like protein family, highly expressed in testis and brain. PUBMED:11376939 EPMC:11376939
Xie L, Chatterjee C, Balsara R, Okeley NM, van der Donk WA; , Biochem Biophys Res Commun 2002;295:952-957.: Heterologous expression and purification of SpaB involved in subtilin biosynthesis. PUBMED:12127987 EPMC:12127987
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007822
The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [PUBMED:11474189, PUBMED:10944443, PUBMED:12566319]; subtilin biosynthesis protein SpaC from Bacillus subtilis [PUBMED:1735728, PUBMED:1539969]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis [PUBMED:1740156]; nisin biosynthesis protein NisC from Lactococcus lactis [PUBMED:8161176, PUBMED:7689965, PUBMED:1482192]; GCR2 from Arabidopsis thaliana [PUBMED:17347412]; and many others.
The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution [PUBMED:16527981]. The globular structure is characterised by an all-alpha fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hyrophobic periodicity has led several authors to claim various members of the family, including eukaryotic LanC-1 and GCR2, to be novel G protein-coupled receptors [PUBMED:17347412, PUBMED:9512664]; some of these claims have since been corrected [PUBMED:10944443, PUBMED:18086512, PUBMED:17894782].
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Curation and family details
|Seed source:||Pfam-B_6095 (release 7.7)|
|Author:||Moxon SJ, Finn RD, Fenech M|
|Number in seed:||47|
|Number in full:||1539|
|Average length of the domain:||282.40 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||54.42 %|
|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:||8|
|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 LANC_like domain has been found. There are 8 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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