2GAF

Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
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: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2gafa_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	mRNA cap methylase	automated matches	(Vaccinia virus ) [TaxId: 10245 ],	SCOPe (2.08)
B [auth D]	d2gafd_	Multi-domain proteins (alpha and beta)	Poly(A) polymerase catalytic subunit-like	Poly(A) polymerase catalytic subunit-like	Poxvirus poly(A) polymerase catalytic subunit-like	Poly(A) polymerase catalytic subunit, PAPL	(Vaccinia virus ) [TaxId: 10245 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	mRNA cap methylase	8073424	4003609	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8073425	3000118	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Family	Poxvirus poly(A) polymerase catalytic domain-like	8055709	4007648	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Family	Poly(A) polymerase C-terminal domain-like	8020519	4002706	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Family	Poxvirus poly(A) polymerase N-terminal domain-like	8055707	4007647	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Superfamily	Nucleotidyltransferase-like	8055710	3000129	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Superfamily	Poly(A) polymerase C-terminal domain-like	8032899	3001629	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Superfamily	Poxvirus poly(A) polymerase N-terminal domain-like	8055708	3002298	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)
A	PF01358	e2gafA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF01358	ECOD (1.6)
B [auth D]	PF12630	e2gafD6	A: alpha arrays	X: N-terminal helical domain in Poxvirus poly(A) polymerase catalytic subunit (From Topology)	H: N-terminal helical domain in Poxvirus poly(A) polymerase catalytic subunit (From Topology)	T: N-terminal helical domain in Poxvirus poly(A) polymerase catalytic subunit	F: PF12630	ECOD (1.6)
B [auth D]	PF03296	e2gafD5	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PF03296	ECOD (1.6)
B [auth D]	PF12629	e2gafD4	A: a+b complex topology	X: C-terminal a+b domain in Poly(A) polymerase catalytic subunit (From Topology)	H: C-terminal a+b domain in Poly(A) polymerase catalytic subunit (From Topology)	T: C-terminal a+b domain in Poly(A) polymerase catalytic subunit	F: PF12629	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
B [auth D]	1.20.1270.320	Mainly Alpha	Up-down Bundle	Substrate Binding Domain Of Dnak	Chain:A	CATH (4.3.0)
B [auth D]	3.30.460.60	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01358	Poly A polymerase regulatory subunit (PARP_regulatory)	Poly A polymerase regulatory subunit	-	Domain
B [auth D]	PF12630	Poxvirus poly(A) polymerase N-terminal domain (Pox_polyA_pol_N)	Poxvirus poly(A) polymerase N-terminal domain	This domain is found at the N-terminus of the pox virus Poly(A) polymerase protein [1]. According to SCOP this domain contains a helix-hairpin-helix motif.	Domain
B [auth D]	PF12629	Poxvirus poly(A) polymerase C-terminal domain (Pox_polyA_pol_C)	Poxvirus poly(A) polymerase C-terminal domain	This domain is found at the C-terminus of the pox virus PolyA polymerase protein [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase	RNA methyltransferase activity O-methyltransferase activity catalytic activity, acting on RNA transferase activity, transferring one-carbon groups catalytic activity, acting on a nucleic acid mRNA (nucleoside-2'-O-)-methyltransferase activity transferase activity S-adenosylmethionine-dependent methyltransferase activity methyltransferase activity catalytic activity mRNA methyltransferase activity translation regulator activity binding organic cyclic compound binding RNA methyltransferase activity O-methyltransferase activity catalytic activity, acting on RNA transferase activity, transferring one-carbon groups catalytic activity, acting on a nucleic acid mRNA (nucleoside-2'-O-)-methyltransferase activity transferase activity S-adenosylmethionine-dependent methyltransferase activity methyltransferase activity catalytic activity mRNA methyltransferase activity 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	cellular biosynthetic process RNA metabolic process 7-methylguanosine RNA capping RNA capping mRNA processing nucleobase-containing compound metabolic process nucleic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process RNA processing 7-methylguanosine mRNA capping cellular metabolic process primary metabolic process gene expression cellular biosynthetic process RNA metabolic process 7-methylguanosine RNA capping RNA capping mRNA processing nucleobase-containing compound metabolic process nucleic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process RNA processing 7-methylguanosine mRNA capping cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process mRNA metabolic process nucleic acid metabolic process organic cyclic compound metabolic process biosynthetic process RNA 5'-end processing metabolic process cellular process macromolecule metabolic process regulation of primary metabolic process regulation of RNA metabolic process RNA 3'-end processing regulation of nucleobase-containing compound metabolic process regulation of mRNA processing regulation of biological process mRNA 3'-end processing regulation of mRNA 3'-end processing biological regulation regulation of macromolecule metabolic process nucleic acid catabolic process regulation of mRNA metabolic process regulation of metabolic process	virion component
B [auth D]	Poly(A) polymerase catalytic subunit	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 poly(A) RNA polymerase activity adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding metal ion binding	cellular biosynthetic process cellular metabolic process RNA metabolic process primary metabolic process gene expression mRNA processing mRNA metabolic process macromolecule biosynthetic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular biosynthetic process cellular metabolic process RNA metabolic process primary metabolic process gene expression mRNA processing mRNA metabolic process macromolecule biosynthetic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process macromolecule metabolic process RNA processing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000176	mRNA methyltransferase-like	Family
A	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A	IPR030375	Poxvirus cap-specific nucleoside 2-O-methyltransferase	Family
A	IPR025804	Poxvirus/kinetoplastid-type cap-specific nucleoside 2-O-methyltransferase	Family
B [auth D]	IPR038337	Poxvirus poly(A) polymerase, catalytic subunit, N-terminal domain superfamily	Homologous Superfamily
B [auth D]	IPR024397	Poxvirus poly(A) polymerase, catalytic subunit, C-terminal	Domain
B [auth D]	IPR004976	Poly(A) polymerase catalytic subunit, Poxvirus	Family
B [auth D]	IPR038419	Poly(A) polymerase, nucleotidyltransferase domain superfamily, Poxvirus	Homologous Superfamily
B [auth D]	IPR024231	Poly(A) polymerase, nucleotidyltransferase domain, Poxvirus	Domain
B [auth D]	IPR037265	Poly(A) polymerase catalytic subunit superfamily	Homologous Superfamily
B [auth D]	IPR024398	Poxvirus poly(A) polymerase, catalytic subunit, N-terminal	Domain

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.