9F37

Replication-like initiation state of influenza polymerase with GTP and CTP at respectively the -1 and +1 positions (strain A/little yellow-shouldered bat/Guatemala/060/2010/H17N10)

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B	PF00602	Influenza RNA-dependent RNA polymerase subunit PB1 (Flu_PB1)	Influenza RNA-dependent RNA polymerase subunit PB1	-	Family
A	PF00603	Influenza RNA-dependent RNA polymerase subunit PA (Flu_PA)	Influenza RNA-dependent RNA polymerase subunit PA	-	Family
C	PF20948	Influenza RNA polymerase PB2 second domain (Flu_PB2_2nd)	Influenza RNA polymerase PB2 second domain	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase ...	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding [1] and endonuclease domains required for transcription initiation by cap-snatching [2]. This entry represents the domain of the Flu PB protein that follows the N-terminal extended region.	Domain
C	PF00604	Influenza RNA polymerase PB2 CAP binding domain (Flu_PB2_5th)	Influenza RNA polymerase PB2 CAP binding domain	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase ...	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding [1] and endonuclease domains required for transcription initiation by cap-snatching [2]. This entry represents the CAP binding domain [2].	Domain
C	PF20947	Influenza RNA polymerase PB2 N-terminal region (Flu_PB2_1st)	Influenza RNA polymerase PB2 N-terminal region	-	Family
C	PF20949	Influenza RNA polymerase PB2 middle domain (Flu_PB2_3rd)	Influenza RNA polymerase PB2 middle domain	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase ...	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding [1] and endonuclease domains required for transcription initiation by cap-snatching [2]. This entry represents the middle domain in Flu PB2 protein.	Domain
C	PF20951	Influenza RNA polymerase PB2 6th domain (Flu_PB2_6th)	Influenza RNA polymerase PB2 6th domain	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase ...	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding [1] and endonuclease domains required for transcription initiation by cap-snatching [2]. This entry represents the 6th domain of PB2.	Domain
C	PF20950	Influenza RNA polymerase PB2 helical domain (Flu_PB2_4th)	Influenza RNA polymerase PB2 helical domain	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase ...	Influenza virus encodes a large, multidomain RNA-dependent RNA polymerase that can both transcribe and replicate the viral RNA genome. In influenza virus, the polymerase is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding [1] and endonuclease domains required for transcription initiation by cap-snatching [2]. This entry represents the helical domain of Flu PB2 protein.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B	RNA-directed RNA polymerase catalytic subunit	5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups RNA binding binding organic cyclic compound binding nucleic acid binding nucleoside phosphate binding 5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups RNA binding binding organic cyclic compound binding nucleic acid binding nucleoside phosphate binding nucleotide binding heterocyclic compound binding small molecule binding	symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process viral genome replication biosynthetic process viral RNA genome replication viral process metabolic process cellular process macromolecule metabolic process viral gene expression viral transcription	host intracellular membrane-bounded organelle host cellular component host intracellular part cellular anatomical structure host cell part host intracellular region host cell nucleus host intracellular organelle intracellular anatomical structure cytoplasm host cell cytoplasm
D [auth R]	3' end of the vRNA promoter	-	-	-
A	Polymerase acidic protein	RNA binding binding organic cyclic compound binding nucleic acid binding cation binding ion binding metal ion binding small molecule binding	viral gene expression viral process viral translational frameshifting viral translation RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process viral genome replication viral gene expression viral process viral translational frameshifting viral translation RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process viral genome replication biosynthetic process viral RNA genome replication metabolic process cellular process macromolecule metabolic process	-
C	Polymerase basic protein 2	RNA binding binding organic cyclic compound binding nucleic acid binding	symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction viral gene expression cap snatching negative stranded viral RNA transcription viral process viral transcription RNA-templated viral transcription 7-methylguanosine mRNA capping symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction viral gene expression cap snatching negative stranded viral RNA transcription viral process viral transcription RNA-templated viral transcription 7-methylguanosine mRNA capping RNA metabolic process primary metabolic process 7-methylguanosine RNA capping RNA capping 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 5'-end processing metabolic process cellular process RNA processing macromolecule metabolic process DNA-templated transcription	host intracellular membrane-bounded organelle host cellular component host intracellular part cellular anatomical structure host cell cytoplasm host cell part host intracellular region host cell mitochondrion host cell cytoplasm part host intracellular organelle host cell nucleus virion component
E [auth V]	5' end of the vRNA promoter	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B	IPR007099	RNA-directed RNA polymerase, negative-strand RNA virus	Domain
B	IPR001407	Influenza RNA-dependent RNA polymerase subunit PB1	Family
A	IPR001009	Influenza RNA-dependent RNA polymerase subunit PA	Family
A	IPR038372	Influenza RNA-dependent RNA polymerase subunit PA, endonuclease domain	Homologous Superfamily
C	IPR049106	Influenza RNA polymerase PB2, N-terminal region	Domain
C	IPR049115	Influenza RNA polymerase PB2, C-terminal domain	Domain
C	IPR049110	Influenza RNA polymerase PB2, second domain	Domain
C	IPR049114	Influenza RNA polymerase PB2, sixth domain	Domain
C	IPR049113	Polymerase basic protein 2, helical domain	Domain
C	IPR049111	Influenza RNA polymerase PB2, middle domain	Domain
C	IPR048298	Influenza RNA polymerase PB2, CAP binding domain	Domain
C	IPR037258	PB2, C-terminal	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.