1Q79

CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1q79a1	All alpha proteins	PAP/OAS1 substrate-binding domain	PAP/OAS1 substrate-binding domain	Poly(A) polymerase, PAP, middle domain	Poly(A) polymerase, PAP, middle domain	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d1q79a3	Alpha and beta proteins (a+b)	Ferredoxin-like	PAP/Archaeal CCA-adding enzyme, C-terminal domain	Poly(A) polymerase, PAP, C-terminal domain	Poly(A) polymerase, PAP, C-terminal domain	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d1q79a2	Alpha and beta proteins (a+b)	Nucleotidyltransferase	Nucleotidyltransferase	Poly(A) polymerase, PAP, N-terminal domain	Poly(A) polymerase, PAP, N-terminal domain	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Poly(A) polymerase, PAP, middle domain	8026121	4002194	SCOP2 (2022-06-29)
A	SCOP2 Family	Poly(A) polymerase, PAP, C-terminal domain	8026122	4001245	SCOP2 (2022-06-29)
A	SCOP2 Family	Poly(A) polymerase, PAP, N-terminal domain	8026123	4002163	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PAP/OAS1 substrate-binding domain-like	8038500	3000941	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PAP/Archaeal CCA-adding enzyme C-terminal domain-like	8038501	3001147	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidyltransferase-like	8038502	3000129	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	PAP_central_2nd	e1q79A1	A: alpha arrays	X: HhH/H2TH	H: SAM/DNA-glycosylase	T: PAP/OAS1 substrate-binding domain	F: PAP_central_2nd	ECOD (1.6)
A	PAP_RNA-bind	e1q79A2	A: a+b two layers	X: Alpha-beta plaits	H: PAP/Archaeal CCA-adding enzyme, C-terminal domain (From Topology)	T: PAP/Archaeal CCA-adding enzyme, C-terminal domain	F: PAP_RNA-bind	ECOD (1.6)
A	PAP_central_1st	e1q79A3	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PAP_central_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.590	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Poly(A) polymerase predicted RNA binding domain	CATH (4.3.0)
A	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (4.3.0)
A	1.10.1410.10	Mainly Alpha	Orthogonal Bundle	Poly(a)-polymerase, middle domain		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04926	Poly(A) polymerase predicted RNA binding domain (PAP_RNA-bind)	Poly(A) polymerase predicted RNA binding domain	Based on its similarity structurally to the RNA recognition motif this domain is thought to be RNA binding [1].	Domain
A	PF04928	Poly(A) polymerase central domain (PAP_central)	Poly(A) polymerase central domain	In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the enzyme at the heart of the polyadenylation machinery, is a templa ...	In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the enzyme at the heart of the polyadenylation machinery, is a template-independent RNA polymerase which specifically incorporates ATP at the 3' end of mRNA [1]. This entry represents the central domain.	Domain
A	PF01909	Nucleotidyltransferase domain (NTP_transf_2)	Nucleotidyltransferase domain	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTa ...	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Poly(A) polymerase alpha	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding manganese ion binding transition metal ion binding poly(A) RNA polymerase activity adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups RNA binding nucleic acid binding	mRNA 3'-end processing co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway RNA metabolic process co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process mRNA processing mRNA metabolic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process mRNA 3'-end processing co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway RNA metabolic process co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process mRNA processing mRNA metabolic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process RNA 3'-end processing metabolic process cellular process RNA processing macromolecule metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007010	Poly(A) polymerase, RNA-binding domain	Domain
A	IPR011068	Nucleotidyltransferase, class I-like, C-terminal	Homologous Superfamily
A	IPR007012	Poly(A) polymerase, central domain	Domain
A	IPR014492	Poly(A) polymerase	Family
A	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
A	IPR048840	Poly(A) polymerase, nucleotidyltransferase domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	CSD	Parent Component: CYS RESID: AA0262 PSI-MOD : L-cysteine sulfinic acid MOD:00267
A	CSO	Parent Component: CYS RESID: AA0262 , AA0205 PSI-MOD : L-cysteine sulfinic acid MOD:00267 , L-cysteine sulfenic acid MOD:00210

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.