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InterPro: IPR017770 RNA 3'-terminal phosphate cyclase, subgroup

Protein matches Help

UniProtKB

Matches:

234 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR017770 RNA3'_term_phos_cycl_sub

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR03399	RNA_3prim_cycl	234
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000228 RNA 3'-terminal phosphate cyclase-like

Children

IPR020723 RNA 3'-terminal phosphate cyclase predicted

Contains

IPR013791 RNA 3'-terminal phosphate cyclase, subset, insert domain
IPR013792 RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR020719 RNA 3'-terminal phosphate cyclase-like, conserved site

GO Term annotation Help

Process

GO:0006396 RNA processing

Function

GO:0003963 RNA-3'-phosphate cyclase activity

Component

GO:0005654 nucleoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Proteins in this entry are RNA 3'-terminal phosphate cyclases (EC:6.5.1.4) whose functions are conserved from Escherichia coli to human. The modification this enzyme performs enables certain RNA ligations to occur, although the full biological role for this enzyme is not fully described.

This entry includes a related enzyme that is present only in eukaryotes, localized to the nucleolus, and involved in ribosomal modification.

RNA 3'-terminal phosphate cyclases catalyse the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.

Structural links Help

PDB - click here

SCOP: c.47.2.1 , d.68.2.1

CATH: 3.30.360.20 , 3.65.10.20

Database links Help

Enzyme: EC:6.5.1.4

CluSTr: ALLvsALL:11181:40.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017770

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00442 RNA 3'-terminal phosphate cyclase

O77264 RNA 3'-terminal phosphate cyclase

P46849 RNA 3'-terminal phosphate cyclase

Q2HJ88 RNA 3'-terminal phosphate cyclase

Q9D7H3 RNA 3'-terminal phosphate cyclase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020723	RNA 3'-terminal phosphate cyclase predicted
IPR016443	RNA 3'-terminal phosphate cyclase-like, eukaryotic
IPR000228	RNA 3'-terminal phosphate cyclase-like
IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR013791	RNA 3'-terminal phosphate cyclase, subset, insert domain
IPR017770	RNA 3'-terminal phosphate cyclase, subgroup
IPR013796	RNA 3'-terminal phosphate cyclase, insert domain
IPR020719	RNA 3'-terminal phosphate cyclase-like, conserved site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Palm GJ, Billy E, Filipowicz W, Wlodawer A. Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology. Structure 8 2000 13-23 [PubMed: 10673421] http://dx.doi.org/10.1016/S0969-2126(00)00076-9

InterPro 23.1