30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner ...
3-578
0e+00
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner for RimO to achieve the modification of ribosomal protein S12. Homologs of YcaO are involved a wide variety of RiPP (ribosomally translated, post-translationally modified peptide) natural product biosynthesis pathways. Some members of this family have an additional N-terminal OsmC-like domain.
:
Pssm-ID: 468680 [Multi-domain] Cd Length: 571 Bit Score: 1113.04 E-value: 0e+00
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner ...
3-578
0e+00
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner for RimO to achieve the modification of ribosomal protein S12. Homologs of YcaO are involved a wide variety of RiPP (ribosomally translated, post-translationally modified peptide) natural product biosynthesis pathways. Some members of this family have an additional N-terminal OsmC-like domain.
Pssm-ID: 468680 [Multi-domain] Cd Length: 571 Bit Score: 1113.04 E-value: 0e+00
YcaO domain protein; This family consists of remarkably well-conserved proteins from gamma and ...
2-576
0e+00
YcaO domain protein; This family consists of remarkably well-conserved proteins from gamma and beta Proteobacteria, heavily skewed towards organisms of marine environments. Its gene neighborhood is not conserved. This family has an OsmC-like N-terminal domain. It shares a YcaO domain, frequently associated with ATP-dependent cyclodehydration for peptide modification. The function is unknown. Fifteen of the first sixteen members of this family are from selenouridine-positive genomes, but this correlation may not be meaningful.
Pssm-ID: 132588 [Multi-domain] Cd Length: 718 Bit Score: 641.88 E-value: 0e+00
YcaO cyclodehydratase C-terminal domain; This is the proline-rich C-terminal domain found in ...
407-581
1.35e-89
YcaO cyclodehydratase C-terminal domain; This is the proline-rich C-terminal domain found in ribosomal protein S12 methylthiotransferase accessory factor YcaO. It has been shown to be involved in both C protein recognition and cyclodehydration. The C-terminal domain resembles a tetratricopeptide repeat that mediates dimerization.
Pssm-ID: 465734 Cd Length: 172 Bit Score: 273.62 E-value: 1.35e-89
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner ...
3-578
0e+00
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO; YcaO acts as a partner for RimO to achieve the modification of ribosomal protein S12. Homologs of YcaO are involved a wide variety of RiPP (ribosomally translated, post-translationally modified peptide) natural product biosynthesis pathways. Some members of this family have an additional N-terminal OsmC-like domain.
Pssm-ID: 468680 [Multi-domain] Cd Length: 571 Bit Score: 1113.04 E-value: 0e+00
YcaO domain protein; This family consists of remarkably well-conserved proteins from gamma and ...
2-576
0e+00
YcaO domain protein; This family consists of remarkably well-conserved proteins from gamma and beta Proteobacteria, heavily skewed towards organisms of marine environments. Its gene neighborhood is not conserved. This family has an OsmC-like N-terminal domain. It shares a YcaO domain, frequently associated with ATP-dependent cyclodehydration for peptide modification. The function is unknown. Fifteen of the first sixteen members of this family are from selenouridine-positive genomes, but this correlation may not be meaningful.
Pssm-ID: 132588 [Multi-domain] Cd Length: 718 Bit Score: 641.88 E-value: 0e+00
YcaO-type kinase domain; This protein family includes YcaO and homologs that can phosphorylate ...
10-404
6.78e-158
YcaO-type kinase domain; This protein family includes YcaO and homologs that can phosphorylate a peptide amide backbone (rather than side chains), as during heterocycle-forming modifications during maturation of the TOMM class (Thiazole/Oxazole-Modified Microcins) of bacteriocins. However, YcaO domain proteins also occur in contexts that do not suggest peptide modification. [Hypothetical proteins, Conserved]
Pssm-ID: 273224 Cd Length: 377 Bit Score: 456.61 E-value: 6.78e-158
YcaO cyclodehydratase C-terminal domain; This is the proline-rich C-terminal domain found in ...
407-581
1.35e-89
YcaO cyclodehydratase C-terminal domain; This is the proline-rich C-terminal domain found in ribosomal protein S12 methylthiotransferase accessory factor YcaO. It has been shown to be involved in both C protein recognition and cyclodehydration. The C-terminal domain resembles a tetratricopeptide repeat that mediates dimerization.
Pssm-ID: 465734 Cd Length: 172 Bit Score: 273.62 E-value: 1.35e-89
YcaO cyclodehydratase, ATP-ad Mg2+-binding; YcaO is an ATP- an Mg2+-binding protein involved ...
58-391
1.04e-82
YcaO cyclodehydratase, ATP-ad Mg2+-binding; YcaO is an ATP- an Mg2+-binding protein involved in the peptidic biosynthesis of azoline. There three motifs involved in the binding are, in UniProtKB:P75838, 71-79: Sx3ExxER, 184-203: Sx6Ex3Qx3ExxER, and 286-290: RxxxE. Three slightly different functional families are represented in this family, proteins involved in TOMM (thiazole/oxazole-modified microcin) biogenesis, non-TOMM proteins such as UniProtKB:P75838, and TfuA-associated non-TOMM proteins involved in trifolitoxin biosynthesis. UniProtKB:P75838 hydrolyses ATP to AMP and pyrophosphate.
Pssm-ID: 426884 Cd Length: 318 Bit Score: 261.45 E-value: 1.04e-82
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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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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