1UMU | pdb_00001umu

STRUCTURE DETERMINATION OF UMUD' BY MAD PHASING OF THE SELENOMETHIONYL PROTEIN

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
B	d1umub_	All beta proteins	LexA/Signal peptidase	LexA/Signal peptidase	LexA-related	UmuD'	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1umua_	All beta proteins	LexA/Signal peptidase	LexA/Signal peptidase	LexA-related	UmuD'	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	LexA/Signal peptidase-like	8043150	3000103	SCOP2B (2022-06-29)
A	SCOP2 Family	LexA endopeptidase domain-like	8030771	4000321	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	LexA/Signal peptidase-like	8043150	3000103	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Peptidase_S24	e1umuB1	A: beta barrels	X: SH3	H: LexA/Signal peptidase (From Topology)	T: LexA/Signal peptidase	F: Peptidase_S24	ECOD (1.6)
A	Peptidase_S24	e1umuA1	A: beta barrels	X: SH3	H: LexA/Signal peptidase (From Topology)	T: LexA/Signal peptidase	F: Peptidase_S24	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.10.109.10	Mainly Beta	Ribbon	Umud Fragment, subunit A	Umud Fragment, subunit A	CATH (4.3.0)
A	2.10.109.10	Mainly Beta	Ribbon	Umud Fragment, subunit A	Umud Fragment, subunit A	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UMUD'	catalytic activity, acting on DNA DNA-directed DNA polymerase activity DNA polymerase activity catalytic activity, acting on a nucleic acid transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups binding nucleic acid binding ATP-dependent activity, acting on DNA ATP-dependent activity peptidase activity serine hydrolase activity catalytic activity, acting on DNA DNA-directed DNA polymerase activity DNA polymerase activity catalytic activity, acting on a nucleic acid transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups binding nucleic acid binding ATP-dependent activity, acting on DNA ATP-dependent activity peptidase activity serine hydrolase activity catalytic activity, acting on a protein serine-type peptidase activity hydrolase activity sequence-specific DNA binding DNA binding identical protein binding protein binding single-stranded DNA binding transcription regulator activity DNA-binding transcription repressor activity DNA-binding transcription factor activity	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process negative regulation of macromolecule metabolic process regulation of biosynthetic process negative regulation of DNA-templated transcription regulation of biological process negative regulation of metabolic process biological regulation primary metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of gene expression biosynthetic process negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process metabolic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of RNA metabolic process DNA metabolic process DNA repair SOS response translesion synthesis DNA damage tolerance DNA synthesis involved in DNA replication DNA replication DNA biosynthetic process proteolysis protein metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex protein-DNA complex transferase complex, transferring phosphorus-containing groups DNA polymerase V complex catalytic complex transferase complex DNA polymerase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015927	Peptidase S24/S26A/S26B/S26C	Domain
A, B	IPR050077	LexA repressor	Family
A, B	IPR039418	LexA-like	Domain
A, B	IPR036286	LexA/Signal peptidase-like superfamily	Homologous Superfamily
A, B	IPR006197	Peptidase S24, LexA-like	Family

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.