SMART: Pfam domain LANC

The domain within your query sequence starts at position 55 and ends at position 173; the E-value for the LANC_like domain shown below is 2.3e-29.

DPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSITFLCGDAGPL
AVAAVLYHKMNSEKQAEECITRLIHLNKIDPHVPNEMLYGRIGYIFALLFVNKNFGEEK

LANC_like

PFAM accession number:	PF05147
Interpro abstract (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) ]. The C terminus of the lantibiotic biosynthesis protein LanM is homologous to LanC [ (PUBMED:19393544) (PUBMED:23071302) ]. LanC-like protein 1 (included in this family) has been shown to function as a glutathione transferase, and as such has been renamed to Glutathione S-transferase LANCL1 [ (PUBMED:19528316) ].

PFAM accession number:

PF05147

Interpro abstract (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) ].

The C terminus of the lantibiotic biosynthesis protein LanM is homologous to LanC [ (PUBMED:19393544) (PUBMED:23071302) ]. LanC-like protein 1 (included in this family) has been shown to function as a glutathione transferase, and as such has been renamed to Glutathione S-transferase LANCL1 [ (PUBMED:19528316) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry LANC_like