6R5K

Cryo-EM structure of a poly(A) RNP bound to the Pan2-Pan3 deadenylase


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF20770e6r5kA3 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF20770ECOD (1.6)
APF13423e6r5kA1 A: a+b complex topologyX: Cysteine proteinases-likeH: Cysteine proteinases (From Topology)T: Cysteine proteinasesF: PF13423ECOD (1.6)
APF00929e6r5kA2 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF00929ECOD (1.6)
D [auth F]PF00076e6r5kF2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
E [auth H]PF00076e6r5kH2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
B [auth D]PF00076e6r5kD2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
F [auth N]PF18101e6r5kN2 A: alpha arraysX: Dimerization domain in caprin-1 and PAN3 (From Topology)H: Dimerization domain in caprin-1 and PAN3 (From Topology)T: Dimerization domain in caprin-1 and PAN3F: PF18101ECOD (1.6)
F [auth N]F_UNCLASSIFIEDe6r5kN1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: F_UNCLASSIFIEDECOD (1.6)
G [auth O]PF18101e6r5kO1 A: alpha arraysX: Dimerization domain in caprin-1 and PAN3 (From Topology)H: Dimerization domain in caprin-1 and PAN3 (From Topology)T: Dimerization domain in caprin-1 and PAN3F: PF18101ECOD (1.6)
G [auth O]F_UNCLASSIFIEDe6r5kO2 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: F_UNCLASSIFIEDECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF20770PAN2 N-terminal (PAN2_N)PAN2 N-terminal- Repeat
PF00929Exonuclease (RNase_T)Exonuclease- Family
PF13423Ubiquitin carboxyl-terminal hydrolase (UCH_1)Ubiquitin carboxyl-terminal hydrolaseThis is the ubiquitin carboxyl-terminal hydrolase domain found in a variety of proteins, including PAN2, one of the subunits of the poly(A)-specific nuclease (PAN) is a deadenylating enzyme involved in cytoplasmic mRNA turnover (consisting of PAN2 an ...This is the ubiquitin carboxyl-terminal hydrolase domain found in a variety of proteins, including PAN2, one of the subunits of the poly(A)-specific nuclease (PAN) is a deadenylating enzyme involved in cytoplasmic mRNA turnover (consisting of PAN2 and PAN3), involved in the initial trimming of poly(A) tails [1-3].
Domain
B [auth D],
D [auth F],
E [auth H]
PF00076RNA recognition motif (RRM_1)RNA recognition motifThe RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and pro ...The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.
Domain
F [auth N]PF18101Pan3 Pseudokinase domain (Pan3_PK)Pan3 Pseudokinase domainThis is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal d ...This is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal domain (C-term). The PAN3 PK domain has retained its ATP binding capacity, and this function is required for mRNA degradation in vivo. Analysis of Pan3 amino acids sequences show that, despite of retaining the general structural characteristics of protein kinases, the PK domain has substitutions in all the conserved motifs that are critical for kinase activity, such as in the catalytic VAIK and HRD motifs and in the Mg2+ binding DFG motif. However, the PAN3 PK domain has been shown to bind ATP. Furthermore, similar to other kinases, the ATP-binding site is located in the cleft between the N- and C-lobes of the kinase fold, however, the ATP-binding pocket is wider than that of typical kinases [3].
Domain
G [auth O]PF18101Pan3 Pseudokinase domain (Pan3_PK)Pan3 Pseudokinase domainThis is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal d ...This is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal domain (C-term). The PAN3 PK domain has retained its ATP binding capacity, and this function is required for mRNA degradation in vivo. Analysis of Pan3 amino acids sequences show that, despite of retaining the general structural characteristics of protein kinases, the PK domain has substitutions in all the conserved motifs that are critical for kinase activity, such as in the catalytic VAIK and HRD motifs and in the Mg2+ binding DFG motif. However, the PAN3 PK domain has been shown to bind ATP. Furthermore, similar to other kinases, the ATP-binding site is located in the cleft between the N- and C-lobes of the kinase fold, however, the ATP-binding pocket is wider than that of typical kinases [3].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
PAN2-PAN3 deadenylation complex catalytic subunit PAN2
B [auth D],
D [auth F],
E [auth H]
Polyadenylate-binding protein, cytoplasmic and nuclear
C [auth E]poly(A) RNA---
F [auth N]PAN2-PAN3 deadenylation complex subunit PAN3
G [auth O]PAN2-PAN3 deadenylation complex subunit PAN3

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR036397Ribonuclease H superfamilyHomologous Superfamily
IPR028889Ubiquitin specific protease domainDomain
IPR030843PAN2-PAN3 deadenylation complex catalytic subunit PAN2Family
IPR028881PAN2, UCH domainDomain
IPR048841PAN2-PAN3 deadenylation complex catalytic subunit PAN2, N-terminalDomain
IPR011047Quinoprotein alcohol dehydrogenase-like superfamilyHomologous Superfamily
IPR038765Papain-like cysteine peptidase superfamilyHomologous Superfamily
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
IPR012337Ribonuclease H-like superfamilyHomologous Superfamily
IPR013520Exonuclease, RNase T/DNA polymerase IIIDomain
B [auth D],
D [auth F],
E [auth H]
IPR006515Polyadenylate binding protein, human types 1, 2, 3, 4Family
B [auth D],
D [auth F],
E [auth H]
IPR002004Polyadenylate-binding protein/Hyperplastic disc proteinDomain
B [auth D],
D [auth F],
E [auth H]
IPR003954RNA recognition motif domain, eukaryoteDomain
B [auth D],
D [auth F],
E [auth H]
IPR000504RNA recognition motif domainDomain
B [auth D],
D [auth F],
E [auth H]
IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
B [auth D],
D [auth F],
E [auth H]
IPR036053PABC (PABP) domainHomologous Superfamily
B [auth D],
D [auth F],
E [auth H]
IPR034364PABP, RNA recognition motif 1Domain
B [auth D],
D [auth F],
E [auth H]
IPR035979RNA-binding domain superfamilyHomologous Superfamily
B [auth D],
D [auth F],
E [auth H]
IPR045305PABP, RNA recognition motif 2Domain
F [auth N]IPR030844PAN2-PAN3 deadenylation complex subunit PAN3Family
F [auth N]IPR000571Zinc finger, CCCH-typeDomain
F [auth N]IPR011009Protein kinase-like domain superfamilyHomologous Superfamily
F [auth N]IPR000719Protein kinase domainDomain
F [auth N]IPR041332Pan3 pseudokinase domainDomain
G [auth O]IPR030844PAN2-PAN3 deadenylation complex subunit PAN3Family
G [auth O]IPR000571Zinc finger, CCCH-typeDomain
G [auth O]IPR011009Protein kinase-like domain superfamilyHomologous Superfamily
G [auth O]IPR000719Protein kinase domainDomain
G [auth O]IPR041332Pan3 pseudokinase domainDomain