1X9A | pdb_00001x9a

Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.

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	d1x9aa_	Alpha and beta proteins (a/b)	DsrEFH-like	DsrEFH-like	DsrH-like	Hypothetical protein TM0979	(Thermotoga maritima ) [TaxId: 2336 ],	SCOPe (2.08)
B	d1x9ab_	Alpha and beta proteins (a/b)	DsrEFH-like	DsrEFH-like	DsrH-like	Hypothetical protein TM0979	(Thermotoga maritima ) [TaxId: 2336 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	DsrH-like	8031407	4003397	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	DsrEFH-like	8043785	3001075	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	DsrEFH-like	8043785	3001075	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	DsrH	e1x9aA1	A: a/b three-layered sandwiches	X: YchN-like (From Topology)	H: YchN-like (From Topology)	T: YchN-like	F: DsrH	ECOD (1.6)
B	DsrH	e1x9aB1	A: a/b three-layered sandwiches	X: YchN-like (From Topology)	H: YchN-like (From Topology)	T: YchN-like	F: DsrH	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1260.10	Alpha Beta	3-Layer(aba) Sandwich	Hypothetical Protein Ychn	Chain: A,	CATH (4.3.0)
B	3.40.1260.10	Alpha Beta	3-Layer(aba) Sandwich	Hypothetical Protein Ychn	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04077	DsrH like protein (DsrH)	DsrH like protein	DsrH is involved in oxidation of intracellular sulphur in the phototrophic sulphur bacterium Chromatium vinosum D [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	hypothetical protein TM0979	-	tRNA thio-modification RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process tRNA processing tRNA wobble base modification RNA processing tRNA modification primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process tRNA thio-modification RNA metabolic process tRNA wobble uridine modification nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process tRNA processing tRNA wobble base modification RNA processing tRNA modification primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process RNA modification biosynthetic process macromolecule modification metabolic process cellular process macromolecule metabolic process tRNA wobble position uridine thiolation	protein-containing complex cellular anatomical structure intracellular anatomical structure catalytic complex sulfurtransferase complex transferase complex cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007215	Sulphur relay, TusB/DsrH	Family
A, B	IPR027396	DsrEFH-like	Homologous Superfamily

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.