4N2P

Structure of Archease from Pyrococcus horikoshii

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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	MTH1598-like	8063583	4003521	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	MTH1598-like	8063584	3000987	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	MTH1598-like	8063584	3000987	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	MTH1598-like	8063584	3000987	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	MTH1598-like	8063584	3000987	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	Archease	e4n2pA2	A: a+b two layers	X: MTH1598-like (From Topology)	H: MTH1598-like (From Topology)	T: MTH1598-like	F: Archease	ECOD (1.6)
B	Archease	e4n2pB1	A: a+b two layers	X: MTH1598-like (From Topology)	H: MTH1598-like (From Topology)	T: MTH1598-like	F: Archease	ECOD (1.6)
C	Archease	e4n2pC1	A: a+b two layers	X: MTH1598-like (From Topology)	H: MTH1598-like (From Topology)	T: MTH1598-like	F: Archease	ECOD (1.6)
D	Archease	e4n2pD1	A: a+b two layers	X: MTH1598-like (From Topology)	H: MTH1598-like (From Topology)	T: MTH1598-like	F: Archease	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.55.10.10	Alpha Beta	3-Layer(bab) Sandwich	Archease, Possible Chaperone	Chain: A	CATH (4.3.0)
B	3.55.10.10	Alpha Beta	3-Layer(bab) Sandwich	Archease, Possible Chaperone	Chain: A	CATH (4.3.0)
C	3.55.10.10	Alpha Beta	3-Layer(bab) Sandwich	Archease, Possible Chaperone	Chain: A	CATH (4.3.0)
D	3.55.10.10	Alpha Beta	3-Layer(bab) Sandwich	Archease, Possible Chaperone	Chain: A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01951	Archease protein family (MTH1598/TM1083) (Archease)	Archease protein family (MTH1598/TM1083)	This archease family of proteins [1], has two SHS2 domains [2], with one inserted into another. It is predicted to be an enzyme [2]. It is predicted to act as a chaperone in DNA/RNA metabolism [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Protein archease	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding	RNA splicing RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process tRNA metabolic process tRNA splicing, via endonucleolytic cleavage and ligation nucleic acid biosynthetic process biosynthetic process RNA splicing, via endonucleolytic cleavage and ligation tRNA processing RNA splicing RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process tRNA metabolic process tRNA splicing, via endonucleolytic cleavage and ligation nucleic acid biosynthetic process biosynthetic process RNA splicing, via endonucleolytic cleavage and ligation tRNA processing metabolic process cellular process RNA processing macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR023572	Archease domain	Domain
A, B, C, D	IPR022952	Archease, archaea	Family
A, B, C, D	IPR002804	Archease	Family
A, B, C, D	IPR036820	Archease domain superfamily	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.