C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
1-613
0e+00
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant.
The actual alignment was detected with superfamily member cd20178:
Pssm-ID: 455131 Cd Length: 652 Bit Score: 1201.59 E-value: 0e+00
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
1-613
0e+00
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.
Pssm-ID: 439131 Cd Length: 652 Bit Score: 1201.59 E-value: 0e+00
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-615
0e+00
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.
Pssm-ID: 462945 Cd Length: 646 Bit Score: 845.73 E-value: 0e+00
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
1-613
0e+00
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.
Pssm-ID: 439131 Cd Length: 652 Bit Score: 1201.59 E-value: 0e+00
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
1-612
0e+00
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant.
Pssm-ID: 439130 Cd Length: 657 Bit Score: 872.36 E-value: 0e+00
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-615
0e+00
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.
Pssm-ID: 462945 Cd Length: 646 Bit Score: 845.73 E-value: 0e+00
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
1-612
0e+00
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L2 (also called protein Dpy-19 homolog 2) deletion is a major cause of globozoospermia.
Pssm-ID: 439132 Cd Length: 652 Bit Score: 827.38 E-value: 0e+00
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
1-612
3.18e-79
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. In humans Dpy19L3 (also called protein Dpy-19 homolog 3) is a C-mannosyltransferase of R-spondin.
Pssm-ID: 439134 Cd Length: 667 Bit Score: 264.01 E-value: 3.18e-79
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
1-578
5.47e-46
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. The function of Dpy19L4 (also called protein Dpy-19 homolog 4) is unknown.
Pssm-ID: 439133 Cd Length: 664 Bit Score: 172.72 E-value: 5.47e-46
Domain of unknown function (DUF6798); This presumed domain is functionally uncharacterized. ...
479-526
8.48e-03
Domain of unknown function (DUF6798); This presumed domain is functionally uncharacterized. This domain family is mainly found in bacteria and archaea, and is approximately 60 amino acids in length. There is a conserved WxxR sequence motif and a conserved Lys residue. Members of this entry may be transmembrane proteins.
Pssm-ID: 466753 [Multi-domain] Cd Length: 60 Bit Score: 34.87 E-value: 8.48e-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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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