6H78

E1 enzyme for ubiquitin like protein activation.

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
H	PF00899	e6h78H1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
I	PF00899	e6h78I1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
N	PF00899	e6h78N1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
A	PF00899	e6h78A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
B	PF00899	e6h78B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
C	PF00899	e6h78C1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
D	PF00899	e6h78D1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
E	PF00899	e6h78E1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
F	PF00899	e6h78F1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
G	PF00899	e6h78G1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
J	PF00899	e6h78J1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
K	PF00899	e6h78K1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
L	PF00899	e6h78L1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
M	PF00899	e6h78M1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
O	PF00899	e6h78O1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)
P	PF00899	e6h78P1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: PF00899	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	PF00899	ThiF family (ThiF)	ThiF family	This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [1-3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Ubiquitin-like modifier-activating enzyme 5	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 identical protein binding protein binding protein homodimerization activity protein dimerization activity UFM1 activating enzyme activity ubiquitin-like modifier activating enzyme activity ligase activity, forming carbon-sulfur bonds catalytic activity, acting on a protein catalytic activity ligase activity ATP-dependent activity cation binding transition metal ion binding zinc ion binding metal ion binding	organonitrogen compound metabolic process primary metabolic process protein ufmylation organic substance metabolic process macromolecule modification metabolic process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein modification by small protein conjugation protein modification by small protein conjugation or removal developmental process multicellular organismal process organonitrogen compound metabolic process primary metabolic process protein ufmylation organic substance metabolic process macromolecule modification metabolic process protein metabolic process macromolecule metabolic process post-translational protein modification protein modification process protein modification by small protein conjugation protein modification by small protein conjugation or removal developmental process multicellular organismal process cellular developmental process homeostatic process hemopoiesis cell development erythrocyte differentiation multicellular organismal-level homeostasis myeloid cell differentiation immune system process cell differentiation anatomical structure development homeostasis of number of cells cellular process myeloid cell homeostasis erythrocyte homeostasis localization cellular response to stimulus response to organic substance regulation of cellular process intracellular receptor signaling pathway response to stimulus response to lipid signaling regulation of signal transduction intracellular estrogen receptor signaling pathway hormone-mediated signaling pathway cell communication cellular response to endogenous stimulus response to hormone response to steroid hormone regulation of intracellular estrogen receptor signaling pathway regulation of intracellular steroid hormone receptor signaling pathway signal transduction cellular response to organic substance cellular response to steroid hormone stimulus response to organic cyclic compound cellular response to hormone stimulus regulation of biological process regulation of signaling response to endogenous stimulus biological regulation cellular response to organic cyclic compound cellular response to chemical stimulus steroid hormone mediated signaling pathway regulation of response to stimulus response to chemical cellular response to lipid nuclear receptor signaling pathway regulation of cell communication intracellular steroid hormone receptor signaling pathway system process nervous system process neuromuscular process megakaryocyte differentiation cellular component disassembly catabolic process macroautophagy cellular metabolic process autophagy cellular component organization cellular catabolic process organelle organization organelle disassembly reticulophagy cellular component organization or biogenesis process utilizing autophagic mechanism cellular response to stress response to stress response to endoplasmic reticulum stress protein polyufmylation protein K69-linked ufmylation	membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system cytosol nucleus organelle subcompartment membrane endoplasmic reticulum subcompartment membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system cytosol nucleus organelle subcompartment membrane endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR045886	ThiF/MoeB/HesA family	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR000594	THIF-type NAD/FAD binding fold	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR029752	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR035985	Ubiquitin-activating enzyme	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Pharos: Q9GZZ9	developmental and epileptic encephalopathy, 44 spinocerebellar ataxia, autosomal recessive 24 cholestasis intellectual disability progressive supranuclear palsy spinocerebellar ataxia type 4 spinocerebellar ataxia type 7 autosomal dominant cerebellar ataxia Chemically-Induced Liver Toxicity epilepsy neurodegenerative disease Pick disease spinocerebellar ataxia type 1 spinocerebellar ataxia type 5 cerebellar ataxia developmental and epileptic encephalopathy, 44 spinocerebellar ataxia, autosomal recessive 24 cholestasis intellectual disability progressive supranuclear palsy spinocerebellar ataxia type 4 spinocerebellar ataxia type 7 autosomal dominant cerebellar ataxia Chemically-Induced Liver Toxicity epilepsy neurodegenerative disease Pick disease spinocerebellar ataxia type 1 spinocerebellar ataxia type 5 cerebellar ataxia ovarian cancer plasma cell myeloma spinocerebellar ataxia type 2 spinocerebellar ataxia type 6 drug-induced liver injury lung cancer pancreatic ductal adenocarcinoma

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.