Summary: Switch protein XOL-1, N-terminal
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This is the Wikipedia entry entitled "XOL-1 Switch protein N-terminal domain". More...
XOL-1 Switch protein N-terminal domain Edit Wikipedia article
Xol-1_N | |||||||||
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![]() crystal structure of xol-1 | |||||||||
Identifiers | |||||||||
Symbol | Xol-1_N | ||||||||
Pfam | PF09108 | ||||||||
Pfam clan | CL0329 | ||||||||
InterPro | IPR015192 | ||||||||
SCOP2 | 1mg7 / SCOPe / SUPFAM | ||||||||
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In molecular biology Xol-1 N is a protein domain, found in the sex-determining protein Xol-1. Xol-1, the master switch gene controlling sex determination and dosage compensation. xol-1 is normally expressed in males, where it promotes male development and prevents dosage compensation.[1]
Function
The function of the Xol-1 protein is to act as a primary sex-determining factor that promotes sexual differentiation. It is required for proper sexual differentiation and male viability. High expression during gastrulation triggers male development, while low expression at that time triggers hermaphrodite development. Although related to GHMP kinase, its mode of action remains unclear.[2]
Structure
adopts a secondary structure consisting of five alpha helices and six antiparallel beta sheets, in a beta-alpha-beta-beta-beta-alpha-beta-alpha-alpha-alpha-beta arrangement. The fold of this family is similar to that found in ribosomal protein S5 domain 2-like.[2] The active site of the enzyme is found at the interface between this domain and the C-terminal GHMP-like domain.
References
- ^ Hargitai B, Kutnyánszky V, Blauwkamp TA, Steták A, Csankovszki G, Takács-Vellai K; et al. (2009). "xol-1, the master sex-switch gene in C. elegans, is a transcriptional target of the terminal sex-determining factor TRA-1". Development. 136 (23): 3881–7. doi:10.1242/dev.034637. PMC 2778738. PMID 19906855.
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(help)CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) - ^ a b Luz JG, Hassig CA, Pickle C, Godzik A, Meyer BJ, Wilson IA (2003). "XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators". Genes Dev. 17 (8): 977–90. doi:10.1101/gad.1082303. PMC 196039. PMID 12672694.
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: CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) Cite error: The named reference "pmid12672694" was defined multiple times with different content (see the help page).
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Switch protein XOL-1, N-terminal Provide feedback
Members of this family, which are required for the formation of the active site of the sex-determining protein Xol-1, adopt a secondary structure consisting of five alpha helices and six antiparallel beta sheets, in a beta-alpha-beta-beta-beta-alpha-beta-alpha-alpha-alpha-beta arrangement. The fold of this family is similar to that found in ribosomal protein S5 domain 2-like [1].
Literature references
-
Luz JG, Hassig CA, Pickle C, Godzik A, Meyer BJ, Wilson IA; , Genes Dev. 2003;17:977-990.: XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators. PUBMED:12672694 EPMC:12672694
External database links
SCOP: | 1mg7 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015192
This domain, found in sex-determining protein Xol-1, adopts a secondary structure consisting of five alpha helices and six antiparallel beta sheets, in a beta-alpha-beta-beta-beta-alpha-beta-alpha-alpha-alpha-beta arrangement. The fold of this family is similar to that found in ribosomal protein S5 domain 2-like [ PUBMED:12672694 ]. The active site of the enzyme is found at the interface between this domain and the C-terminal GHMP-like domain.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan S5 (CL0329), which has the following description:
This superfamily contains a wide range of families that possess a structure similar to the second domain of ribosomal S5 protein.
The clan contains the following 18 members:
ChlI DNA_gyraseB DNA_mis_repair EFG_IV Fae GalKase_gal_bdg GHMP_kinases_N IGPD Lon_C LpxC Morc6_S5 Ribonuclease_P Ribosomal_S5_C Ribosomal_S9 RNase_PH Topo-VIb_trans UPF0029 Xol-1_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (2) |
Full (18) |
Representative proteomes | UniProt (34) |
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RP15 (1) |
RP35 (2) |
RP55 (18) |
RP75 (18) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (2) |
Full (18) |
Representative proteomes | UniProt (34) |
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RP15 (1) |
RP35 (2) |
RP55 (18) |
RP75 (18) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | pdb_1mg7 |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Sammut SJ |
Number in seed: | 2 |
Number in full: | 18 |
Average length of the domain: | 146.8 aa |
Average identity of full alignment: | 25 % |
Average coverage of the sequence by the domain: | 37.97 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 160 | ||||||||||||
Family (HMM) version: | 13 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Xol-1_N domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
Protein | Predicted structure | External Information |
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Q23229 | View 3D Structure | Click here |
Q611X0 | View 3D Structure | Click here |