Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
74-407
9.53e-151
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were 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. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.
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Pssm-ID: 271202 Cd Length: 349 Bit Score: 430.59 E-value: 9.53e-151
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
13-101
7.66e-06
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
The actual alignment was detected with superfamily member cd04791:
Pssm-ID: 471159 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 7.66e-06
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
74-407
9.53e-151
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were 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. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.
Pssm-ID: 271202 Cd Length: 349 Bit Score: 430.59 E-value: 9.53e-151
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
67-411
4.08e-127
Lanthionine synthetase C-like protein; 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.
Pssm-ID: 398697 [Multi-domain] Cd Length: 350 Bit Score: 370.56 E-value: 4.08e-127
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
74-395
8.46e-23
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274840 [Multi-domain] Cd Length: 931 Bit Score: 100.80 E-value: 8.46e-23
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
13-101
7.66e-06
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 7.66e-06
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
74-407
9.53e-151
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were 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. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.
Pssm-ID: 271202 Cd Length: 349 Bit Score: 430.59 E-value: 9.53e-151
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
67-411
4.08e-127
Lanthionine synthetase C-like protein; 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.
Pssm-ID: 398697 [Multi-domain] Cd Length: 350 Bit Score: 370.56 E-value: 4.08e-127
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
74-408
9.19e-69
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
Pssm-ID: 271198 [Multi-domain] Cd Length: 351 Bit Score: 221.22 E-value: 9.19e-69
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
74-395
8.46e-23
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274840 [Multi-domain] Cd Length: 931 Bit Score: 100.80 E-value: 8.46e-23
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
74-403
1.07e-22
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 100.47 E-value: 1.07e-22
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
75-398
8.20e-12
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans) in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs.
Pssm-ID: 271201 Cd Length: 377 Bit Score: 66.22 E-value: 8.20e-12
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
74-407
9.80e-08
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 9.80e-08
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
13-101
7.66e-06
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 7.66e-06
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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