Annotations: 5IZM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	GTP_EFTU_D2_1	e5izmA3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2_1	ECOD (1.6)
A	KOG0461	e5izmA4	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: KOG0461	ECOD (1.6)
A	eSelB_III	e5izmA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Aminomethyltransferase beta-barrel domain	F: eSelB_III	ECOD (1.6)
A	MnmE_helical_2nd	e5izmA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
B	GTP_EFTU_D2_1	e5izmB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2_1	ECOD (1.6)
B	KOG0461	e5izmB4	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: KOG0461	ECOD (1.6)
B	eSelB_III	e5izmB2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Aminomethyltransferase beta-barrel domain	F: eSelB_III	ECOD (1.6)
B	MnmE_helical_2nd	e5izmB3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00009	Elongation factor Tu GTP binding domain (GTP_EFTU)	Elongation factor Tu GTP binding domain	This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.	Domain
A, B	PF21131	eEFSec C-terminal RIFT domain (eEFSec_4th)	eEFSec C-terminal RIFT domain	This entry represents the C-terminal RIFT beta barrel domain found in the Selenocysteine-specific elongation factor eEFSec [1]. Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the c ...	This entry represents the C-terminal RIFT beta barrel domain found in the Selenocysteine-specific elongation factor eEFSec [1]. Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal stop codon. A specialised translation elongation factor, eEFSec in eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins [1].	Domain
A, B	PF21208	Selenocysteine-specific elongation factor, eukaryotes, 3rd domain (euk_SelB_III)	Selenocysteine-specific elongation factor, eukaryotes, 3rd domain	This domain is found in Selenocysteine-specific elongation factor from humans (SelB) and similar sequences from eukaryotes. SelB is a translation factor necessary for the incorporation of selenocysteine into proteins. This protein adopts a chalice-li ...	This domain is found in Selenocysteine-specific elongation factor from humans (SelB) and similar sequences from eukaryotes. SelB is a translation factor necessary for the incorporation of selenocysteine into proteins. This protein adopts a chalice-like structure composed of four domains. This entry represents the third domain, which shows seven antiparallel beta-strands and a long alpha-helix [1].	Domain
A, B	PF03144	Elongation factor Tu domain 2 (GTP_EFTU_D2)	Elongation factor Tu domain 2	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Selenocysteine-specific elongation factor	translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding selenocysteine insertion sequence binding RNA binding mRNA binding ribonucleoprotein complex binding protein-containing complex binding tRNA binding guanyl nucleotide binding translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding selenocysteine insertion sequence binding RNA binding mRNA binding ribonucleoprotein complex binding protein-containing complex binding tRNA binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	selenocysteine incorporation regulation of cellular process cellular biosynthetic process organonitrogen compound biosynthetic process regulation of primary metabolic process post-transcriptional regulation of gene expression organic substance metabolic process organic substance biosynthetic process protein metabolic process regulation of biosynthetic process regulation of biological process organonitrogen compound metabolic process cellular metabolic process regulation of protein metabolic process selenocysteine incorporation regulation of cellular process cellular biosynthetic process organonitrogen compound biosynthetic process regulation of primary metabolic process post-transcriptional regulation of gene expression organic substance metabolic process organic substance biosynthetic process protein metabolic process regulation of biosynthetic process regulation of biological process organonitrogen compound metabolic process cellular metabolic process regulation of protein metabolic process biological regulation regulation of cellular metabolic process primary metabolic process regulation of macromolecule metabolic process translational readthrough gene expression translation macromolecule biosynthetic process regulation of cellular biosynthetic process regulation of gene expression biosynthetic process regulation of translation translational elongation regulation of macromolecule biosynthetic process metabolic process cellular process macromolecule metabolic process regulation of metabolic process	protein-containing complex ribonucleoprotein complex intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR049393	Selenocysteine-specific elongation factor, 3rd domain	Domain
A, B	IPR000795	Translational (tr)-type GTP-binding domain	Domain
A, B	IPR049394	Selenocysteine-specific elongation factor, C-terminal RIFT domain	Domain
A, B	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
A, B	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P57772	hypospadias chronic obstructive pulmonary disease Chronic Airflow Obstruction prostate carcinoma

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.