2LGT | pdb_00002lgt

Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1	8035419	3001963	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	eRF1_1_1	e2lgtA1	A: a+b three layers	X: N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1 (From Topology)	H: N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1 (From Topology)	T: N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1	F: eRF1_1_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.960.10	Alpha Beta	2-Layer Sandwich	Translation, Eukaryotic Peptide Chain Release Factor Subunit 1	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF03463	eRF1 domain 1 (eRF1_1)	eRF1 domain 1	The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [1]. The o ...	The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [1]. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site [1]. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Eukaryotic peptide chain release factor subunit 1	translation release factor activity, codon specific translation factor activity translation release factor activity translation termination factor activity ribonucleoprotein complex binding protein-containing complex binding binding ribosome binding hydrolase activity, acting on ester bonds catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid carboxylic ester hydrolase activity hydrolase activity catalytic activity, acting on a tRNA translation release factor activity, codon specific translation factor activity translation release factor activity translation termination factor activity ribonucleoprotein complex binding protein-containing complex binding binding ribosome binding hydrolase activity, acting on ester bonds catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid carboxylic ester hydrolase activity hydrolase activity catalytic activity, acting on a tRNA peptidyl-tRNA hydrolase activity catalytic activity RNA binding nucleic acid binding sequence-specific mRNA binding mRNA binding	cellular component disassembly cytoplasmic translational termination protein-containing complex organization protein-containing complex disassembly primary metabolic process translation gene expression macromolecule biosynthetic process cellular component organization biosynthetic process cytoplasmic translation cellular process metabolic process translational termination cellular component disassembly cytoplasmic translational termination protein-containing complex organization protein-containing complex disassembly primary metabolic process translation gene expression macromolecule biosynthetic process cellular component organization biosynthetic process cytoplasmic translation cellular process metabolic process translational termination cellular component organization or biogenesis protein metabolic process macromolecule metabolic process protein methylation macromolecule methylation protein alkylation methylation macromolecule modification protein modification process regulation of cellular process regulation of cellular component organization regulation of protein-containing complex disassembly regulation of primary metabolic process post-transcriptional regulation of gene expression regulation of biosynthetic process regulation of biological process regulation of protein metabolic process regulation of translational termination biological regulation regulation of macromolecule metabolic process regulation of gene expression regulation of translation regulation of macromolecule biosynthetic process regulation of metabolic process catabolic process nuclear-transcribed mRNA catabolic process, nonsense-mediated decay negative regulation of biological process RNA metabolic process macromolecule catabolic process nucleobase-containing compound metabolic process negative regulation of cellular process RNA catabolic process negative regulation of macromolecule metabolic process mRNA catabolic process nuclear-transcribed mRNA catabolic process negative regulation of metabolic process mRNA metabolic process nucleic acid metabolic process nucleobase-containing compound catabolic process negative regulation of gene expression negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process nucleic acid catabolic process	intracellular organelle cellular anatomical structure intracellular anatomical structure cytosolic ribosome organelle membraneless organelle intracellular membraneless organelle ribosome cytoplasm cytosol protein-containing complex translation release factor complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR004403	Peptide chain release factor eRF1/aRF1	Family
A	IPR005141	eRF1 domain 2	Domain
A	IPR005140	eRF1 domain 1/Pelota-like	Domain
A	IPR042226	eRF1, domain 2 superfamily	Homologous Superfamily
A	IPR024049	eRF1, domain 1	Homologous Superfamily
A	IPR005142	eRF1 domain 3	Domain
A	IPR029064	Ribosomal protein eL30-like superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P62495	autism spectrum disorder myopathy breast cancer ovarian cancer diabetes mellitus plasma cell myeloma

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.