1MG7 | pdb_00001mg7

Crystal Structure of xol-1

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1mg7a1	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	Early switch protein XOL-1, N-terminal domain	Early switch protein XOL-1, N-terminal domain	(Caenorhabditis elegans ) [TaxId: 6239 ],	SCOPe (2.08)
A	d1mg7a2	Alpha and beta proteins (a+b)	Ferredoxin-like	GHMP Kinase, C-terminal domain	Early switch protein XOL-1	Early switch protein XOL-1	(Caenorhabditis elegans ) [TaxId: 6239 ],	SCOPe (2.08)
B	d1mg7b1	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	Early switch protein XOL-1, N-terminal domain	Early switch protein XOL-1, N-terminal domain	(Caenorhabditis elegans ) [TaxId: 6239 ],	SCOPe (2.08)
B	d1mg7b2	Alpha and beta proteins (a+b)	Ferredoxin-like	GHMP Kinase, C-terminal domain	Early switch protein XOL-1	Early switch protein XOL-1	(Caenorhabditis elegans ) [TaxId: 6239 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GHMP Kinase, C-terminal domain	8032846	3001245	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8032845	3000100	SCOP2B (2022-06-29)
B	SCOP2 Family	Early switch protein XOL-1, N-terminal domain	8020465	4000576	SCOP2 (2022-06-29)
B	SCOP2 Family	Early switch protein XOL-1	8020466	4000645	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Ribosomal protein S5 domain 2-like	8032845	3000100	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	GHMP Kinase, C-terminal domain	8032846	3001245	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Xol-1_N	e1mg7A2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Xol-1_N	ECOD (1.6)
A	Xol-1_GHMP-like	e1mg7A1	A: a+b two layers	X: Alpha-beta plaits	H: GHMP Kinase, C-terminal domain (From Topology)	T: GHMP Kinase, C-terminal domain	F: Xol-1_GHMP-like	ECOD (1.6)
B	Xol-1_N	e1mg7B2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Xol-1_N	ECOD (1.6)
B	Xol-1_GHMP-like	e1mg7B1	A: a+b two layers	X: Alpha-beta plaits	H: GHMP Kinase, C-terminal domain (From Topology)	T: GHMP Kinase, C-terminal domain	F: Xol-1_GHMP-like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.1000	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Switch protein XOL-1, GHMP-like	CATH (4.3.0)
A	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
B	3.30.70.1000	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Switch protein XOL-1, GHMP-like	CATH (4.3.0)
B	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF09108	Switch protein XOL-1, N-terminal (Xol-1_N)	Switch protein XOL-1, N-terminal	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- ...	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].	Domain
A, B	PF09109	Switch protein XOL-1, GHMP-like (Xol-1_GHMP-like)	Switch protein XOL-1, GHMP-like	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 seven antiparallel beta sheets, in a beta-alpha-beta-alpha-alpha-al ...	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 seven antiparallel beta sheets, in a beta-alpha-beta-alpha-alpha-alpha-beta-beta-alpha-beta-beta-beta arrangement. The fold of this family is structurally similar to that found in the C-terminal domain of GHMP Kinase [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	early switch protein xol-1 2.2k splice form	-	regulation of biosynthetic process dosage compensation by hypoactivation of X chromosome regulation of biological process regulation of cellular process sex-chromosome dosage compensation epigenetic regulation of gene expression biological regulation regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process cellular component organization regulation of gene expression biosynthetic process chromatin organization chromatin remodeling regulation of biosynthetic process dosage compensation by hypoactivation of X chromosome regulation of biological process regulation of cellular process sex-chromosome dosage compensation epigenetic regulation of gene expression biological regulation regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process cellular component organization regulation of gene expression biosynthetic process chromatin organization chromatin remodeling cellular process regulation of macromolecule biosynthetic process metabolic process cellular component organization or biogenesis macromolecule metabolic process regulation of metabolic process developmental process cellular developmental process cell differentiation alternative mRNA splicing, via spliceosome RNA metabolic process mRNA processing nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process RNA processing RNA splicing primary metabolic process nucleobase-containing compound biosynthetic process mRNA metabolic process nucleic acid metabolic process RNA splicing, via transesterification reactions mRNA splicing, via spliceosome mRNA alternative trans-splicing RNA splicing, via transesterification reactions with bulged adenosine as nucleophile mRNA trans splicing, via spliceosome multicellular organism development multicellular organismal process sex determination male sex determination reproductive process anatomical structure development developmental process involved in reproduction	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015193	Switch protein XOL-1, GHMP-like	Domain
A, B	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A, B	IPR036554	GHMP kinase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	Homologous Superfamily
A, B	IPR015192	Switch protein XOL-1, N-terminal	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.