Annotations: 2GIA

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
D [auth G]	d2giag_	Alpha and beta proteins (a+b)	ssDNA-binding transcriptional regulator domain	ssDNA-binding transcriptional regulator domain	Guide RNA binding protein gBP	Guide RNA binding protein gBP25	(Trypanosoma brucei brucei TREU927 ) [TaxId: 185431 ],	SCOPe (2.08)
A	d2giaa1	Alpha and beta proteins (a+b)	ssDNA-binding transcriptional regulator domain	ssDNA-binding transcriptional regulator domain	Guide RNA binding protein gBP	Guide RNA binding protein gBP25	(Trypanosoma brucei brucei TREU927 ) [TaxId: 185431 ],	SCOPe (2.08)
B	d2giab1	Alpha and beta proteins (a+b)	ssDNA-binding transcriptional regulator domain	ssDNA-binding transcriptional regulator domain	Guide RNA binding protein gBP	GBP21	(Trypanosoma brucei brucei TREU927 ) [TaxId: 185431 ],	SCOPe (2.08)
C [auth D]	d2giad_	Alpha and beta proteins (a+b)	ssDNA-binding transcriptional regulator domain	ssDNA-binding transcriptional regulator domain	Guide RNA binding protein gBP	GBP21	(Trypanosoma brucei brucei TREU927 ) [TaxId: 185431 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D [auth G]	SCOP2B Superfamily	ssDNA-binding transcriptional regulator domain	8041898	3000513	SCOP2B (2022-06-29)
A	SCOP2 Family	Guide RNA binding protein gBP	8029519	4003411	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ssDNA-binding transcriptional regulator domain	8041898	3000513	SCOP2 (2022-06-29)
B	SCOP2 Family	Guide RNA binding protein gBP	8029520	4003411	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	ssDNA-binding transcriptional regulator domain	8041899	3000513	SCOP2 (2022-06-29)
C [auth D]	SCOP2B Superfamily	ssDNA-binding transcriptional regulator domain	8041899	3000513	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
D [auth G]	PF09387	e2giaG1	A: a+b two layers	X: ssDNA-binding transcriptional regulator domain-like	H: ssDNA-binding transcriptional regulator domain (From Topology)	T: ssDNA-binding transcriptional regulator domain	F: PF09387	ECOD (1.6)
A	PF09387	e2giaA1	A: a+b two layers	X: ssDNA-binding transcriptional regulator domain-like	H: ssDNA-binding transcriptional regulator domain (From Topology)	T: ssDNA-binding transcriptional regulator domain	F: PF09387	ECOD (1.6)
B	PF09387	e2giaB1	A: a+b two layers	X: ssDNA-binding transcriptional regulator domain-like	H: ssDNA-binding transcriptional regulator domain (From Topology)	T: ssDNA-binding transcriptional regulator domain	F: PF09387	ECOD (1.6)
C [auth D]	PF09387	e2giaD1	A: a+b two layers	X: ssDNA-binding transcriptional regulator domain-like	H: ssDNA-binding transcriptional regulator domain (From Topology)	T: ssDNA-binding transcriptional regulator domain	F: PF09387	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D [auth G]	2.30.31.40	Mainly Beta	Roll	Transcriptional Co-activator pc4	Chain A	CATH (4.3.0)
A	2.30.31.40	Mainly Beta	Roll	Transcriptional Co-activator pc4	Chain A	CATH (4.3.0)
B	2.30.31.40	Mainly Beta	Roll	Transcriptional Co-activator pc4	Chain A	CATH (4.3.0)
C [auth D]	2.30.31.40	Mainly Beta	Roll	Transcriptional Co-activator pc4	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, D [auth G]	PF09387	Mitochondrial RNA binding protein MRP (MRP)	Mitochondrial RNA binding protein MRP	MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilises them in an unfolded conformation suitable for RNA-RNA hybridisation. Each MRP subunit ad ...	MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilises them in an unfolded conformation suitable for RNA-RNA hybridisation. Each MRP subunit adopts a 'whirly' transcription factor fold [1].	Domain
B, C [auth D]	PF09387	Mitochondrial RNA binding protein MRP (MRP)	Mitochondrial RNA binding protein MRP	MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilises them in an unfolded conformation suitable for RNA-RNA hybridisation. Each MRP subunit ad ...	MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilises them in an unfolded conformation suitable for RNA-RNA hybridisation. Each MRP subunit adopts a 'whirly' transcription factor fold [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, D [auth G]	mitochondrial RNA-binding protein 2	DNA binding binding organic cyclic compound binding nucleic acid binding RNA binding mRNA binding	regulation of cellular process cellular biosynthetic process RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process organic substance metabolic process organic substance biosynthetic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of cellular process cellular biosynthetic process RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process organic substance metabolic process organic substance biosynthetic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process cellular metabolic process biological regulation primary metabolic process regulation of cellular metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process organic cyclic compound metabolic process regulation of gene expression biosynthetic process organic cyclic compound biosynthetic process metabolic process regulation of macromolecule biosynthetic process cellular process regulation of DNA-templated transcription macromolecule metabolic process regulation of metabolic process mRNA modification mRNA metabolic process RNA modification macromolecule modification nucleic acid catabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle kinetoplast
B, C [auth D]	mitochondrial RNA-binding protein 1	DNA binding binding organic cyclic compound binding nucleic acid binding RNA binding mRNA binding	regulation of cellular process cellular biosynthetic process RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process organic substance metabolic process organic substance biosynthetic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of cellular process cellular biosynthetic process RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process organic substance metabolic process organic substance biosynthetic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process cellular metabolic process biological regulation primary metabolic process regulation of cellular metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process organic cyclic compound metabolic process regulation of gene expression biosynthetic process organic cyclic compound biosynthetic process metabolic process regulation of macromolecule biosynthetic process cellular process regulation of DNA-templated transcription macromolecule metabolic process regulation of metabolic process post-transcriptional regulation of gene expression mRNA modification mRNA metabolic process RNA modification macromolecule modification nucleic acid catabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, D [auth G]	IPR009044	ssDNA-binding transcriptional regulator	Homologous Superfamily
A, D [auth G]	IPR032680	SUN domain-containing protein 1, N-terminal	Domain
B, C [auth D]	IPR009044	ssDNA-binding transcriptional regulator	Homologous Superfamily
B, C [auth D]	IPR032680	SUN domain-containing protein 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 R01GM133198.