Annotations: 5GHA

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01171	e5ghaA2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF01171	ECOD (1.6)
A	F_UNCLASSIFIED	e5ghaA3	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF22082	e5ghaA1	A: few secondary structure elements	X: Glucocorticoid receptor-like	H: LIM domain-like	T: LIM domain-like	F: PF22082	ECOD (1.6)
B [auth D]	PF01171	e5ghaD3	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF01171	ECOD (1.6)
B [auth D]	PF02132	e5ghaD1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: PF02132	ECOD (1.6)
B [auth D]	PF22082	e5ghaD2	A: few secondary structure elements	X: Glucocorticoid receptor-like	H: LIM domain-like	T: LIM domain-like	F: PF22082	ECOD (1.6)
C [auth B]	PF01171	e5ghaB2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF01171	ECOD (1.6)
C [auth B]	PF02132	e5ghaB1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: PF02132	ECOD (1.6)
C [auth B]	PF22082	e5ghaB3	A: few secondary structure elements	X: Glucocorticoid receptor-like	H: LIM domain-like	T: LIM domain-like	F: PF22082	ECOD (1.6)
D [auth C]	PF01171	e5ghaC3	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF01171	ECOD (1.6)
D [auth C]	PF02132	e5ghaC1	A: few secondary structure elements	X: RING/U-box-like	H: RING/U-box-like	T: RING/U-box	F: PF02132	ECOD (1.6)
D [auth C]	PF22082	e5ghaC2	A: few secondary structure elements	X: Glucocorticoid receptor-like	H: LIM domain-like	T: LIM domain-like	F: PF22082	ECOD (1.6)
E	PF02597	e5ghaE1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: PF02597	ECOD (1.6)
F [auth H]	F_UNCLASSIFIED	e5ghaH1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: F_UNCLASSIFIED	ECOD (1.6)
G [auth F]	F_UNCLASSIFIED	e5ghaF1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: F_UNCLASSIFIED	ECOD (1.6)
H [auth G]	PF02597	e5ghaG1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: PF02597	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B [auth D]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
C [auth B]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D [auth C]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth D], C [auth B], D [auth C]	PF01171	PP-loop family (ATP_bind_3)	PP-loop family	-	Family
E, F [auth H], G [auth F], H [auth G]	PF02597	ThiS family (ThiS)	ThiS family	ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer Swiss:O32583. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the a ...	ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer Swiss:O32583. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalysed by IscS [1]. MoaD, Swiss:P30748 a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth D], C [auth B], D [auth C]	Sulfur Transferase TtuA	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding RNA binding tRNA binding nucleic acid binding cation binding metal ion binding transferase activity catalytic activity	tRNA thio-modification cellular biosynthetic process RNA metabolic process nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA thio-modification cellular biosynthetic process RNA metabolic process nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process 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 tRNA wobble uridine modification tRNA wobble base modification	-
E, F [auth H], G [auth F], H [auth G]	Sulfur Carrier TtuB	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	cellular biosynthetic process cellular metabolic process RNA metabolic process primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process tRNA processing ncRNA metabolic process organic substance biosynthetic process cellular biosynthetic process cellular metabolic process RNA metabolic process primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process tRNA processing ncRNA metabolic process organic substance biosynthetic process nucleic acid catabolic process metabolic process cellular process macromolecule metabolic process RNA processing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth D], C [auth B], D [auth C]	IPR011063	tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal	Domain
A, B [auth D], C [auth B], D [auth C]	IPR035107	tRNA thiolation protein, TtcA/Ctu1 type	Family
A, B [auth D], C [auth B], D [auth C]	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A, B [auth D], C [auth B], D [auth C]	IPR000541	Cytoplasmic tRNA 2-thiolation protein 1	Family
E, F [auth H], G [auth F], H [auth G]	IPR003749	Sulfur carrier ThiS/MoaD-like	Family
E, F [auth H], G [auth F], H [auth G]	IPR016155	Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp	Homologous Superfamily
E, F [auth H], G [auth F], H [auth G]	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.