Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
605-1151
3.98e-128
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 pfam07944:
Pssm-ID: 471159 [Multi-domain] Cd Length: 503 Bit Score: 410.93 E-value: 3.98e-128
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
336-419
9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
:
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 122.61 E-value: 9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
426-509
2.42e-26
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
:
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 104.12 E-value: 2.42e-26
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
519-576
5.94e-10
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
:
Pssm-ID: 400079 [Multi-domain] Cd Length: 59 Bit Score: 56.56 E-value: 5.94e-10
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ...
1548-1593
1.46e-03
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
:
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 38.84 E-value: 1.46e-03
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
605-1151
3.98e-128
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
Pssm-ID: 400342 [Multi-domain] Cd Length: 503 Bit Score: 410.93 E-value: 3.98e-128
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
336-419
9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 122.61 E-value: 9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
426-509
2.42e-26
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 104.12 E-value: 2.42e-26
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
519-576
5.94e-10
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
Pssm-ID: 400079 [Multi-domain] Cd Length: 59 Bit Score: 56.56 E-value: 5.94e-10
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ...
1548-1593
1.46e-03
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 38.84 E-value: 1.46e-03
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
605-1151
3.98e-128
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
Pssm-ID: 400342 [Multi-domain] Cd Length: 503 Bit Score: 410.93 E-value: 3.98e-128
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
336-419
9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 122.61 E-value: 9.31e-33
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial ...
426-509
2.42e-26
Atrophied bacterial Ig domain; This domain is related to pfam02368 a bacterial immunoglobulin-like domain. According to structure predictions members of this domain family have lost several beta strands found on one sheet of the Ig domain. This domain is found in a wide range of bacterial cell surface proteins.
Pssm-ID: 466727 [Multi-domain] Cd Length: 89 Bit Score: 104.12 E-value: 2.42e-26
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ...
519-576
5.94e-10
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
Pssm-ID: 400079 [Multi-domain] Cd Length: 59 Bit Score: 56.56 E-value: 5.94e-10
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ...
1548-1593
1.46e-03
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 38.84 E-value: 1.46e-03
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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