Annotations: 3G05

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	GidA-like	8049418	4006485	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thi4/GidA-like	8092226	3000051	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Helix-hairpin-helix tandem	8092230	3000163	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thi4/GidA-like	8092226	3000051	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Helix-hairpin-helix tandem	8092230	3000163	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)
A	PF21680	e3g05A8	A: alpha arrays	X: C-terminal helical domain in tRNA modifying enzyme GidA (From Topology)	H: C-terminal helical domain in tRNA modifying enzyme GidA (From Topology)	T: C-terminal helical domain in tRNA modifying enzyme GidA	F: PF21680	ECOD (1.6)
A	PF01134	e3g05A7	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: PF01134	ECOD (1.6)
A	PF01134	e3g05A6	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF01134	ECOD (1.6)
B	PF21680	e3g05B8	A: alpha arrays	X: C-terminal helical domain in tRNA modifying enzyme GidA (From Topology)	H: C-terminal helical domain in tRNA modifying enzyme GidA (From Topology)	T: C-terminal helical domain in tRNA modifying enzyme GidA	F: PF21680	ECOD (1.6)
B	PF01134	e3g05B7	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: PF01134	ECOD (1.6)
B	PF01134	e3g05B6	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF01134	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.30.260	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
B	2.40.30.260	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21680	tRNA modifying enzyme MnmG/GidA C-terminal helical domain (GIDA_C_1st)	tRNA modifying enzyme MnmG/GidA C-terminal helical domain	The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and m ...	The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA [2] and, in particular the small bundle, to be responsible for the interaction with protein MnmE [1]. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, Pfam:PF12631. This entry represents the first helices of the GidA associated domain. The last three helices are covered in Pfam:PF13932.	Domain
A, B	PF01134	Glucose inhibited division protein A (GIDA)	Glucose inhibited division protein A	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG	flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	cellular biosynthetic process RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process tRNA wobble base modification RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process cellular biosynthetic process RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process tRNA wobble base modification RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process RNA modification biosynthetic process ncRNA metabolic process macromolecule modification nucleic acid catabolic process metabolic process cellular process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR047001	tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal subdomain	Domain
A, B	IPR040131	MnmG, N-terminal domain	Domain
A, B	IPR049312	tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal, N-terninal subdomain	Domain
A, B	IPR026904	tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG, C-terminal	Domain
A, B	IPR044920	tRNA uridine 5-carboxymethylaminomethyl modification enzyme, C-terminal subdomain superfamily	Homologous Superfamily
A, B	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR002218	tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG-related	Family
A, B	IPR004416	tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG	Family
A, B	IPR020595	MnmG-related, conserved site	Conserved Site

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.