SMART: Pfam domain PTS

The domain within your query sequence starts at position 21 and ends at position 198; the E-value for the PTS_2-RNA domain shown below is 2.6e-67.

DRNVQLSKALSYALRHGALKLGLPMRADGFVPLQALLQLPQFHSFSIEDVQLVVNTNEKQ
RFTLQPGEPSTGLLIRANQGHSLQVPELELTPLETPQALPLTLVHGTFWKHWPSILLKGL
SRQGRTHIHLASGLPGDPGVISGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPG

PTS_2-RNA

PFAM accession number:	PF01885
Interpro abstract (IPR002745):	This entry includes Tpt1 and its homologues from all domains of life. Tpt1 was first discovered as an essential component of the fungal tRNA splicing pathway, which characteristically generates a 2'-PO4, 3'-5' phosphodiester splice junction during the tRNA ligation reaction [ (PUBMED:2154680) ]. It is an enzyme that catalyzes the transfer of an internal RNA 2'-monophosphate (2'-PO4) to NAD+ to form a 2'-OH RNA, ADP-ribose 1"-2" cyclic phosphate, and nicotinamide [ (PUBMED:8392224) ]. Interestingly, many Tpt1 homologues have no obvious need for an RNA 2'-phosphotransferase because: (i) they lack tRNA introns; and/or (ii) they are not known to have an enzymatic pathway that generates 2'-PO4, 3'-5' phosphodiester RNA structures. There are more evidence showing that Tpt1 homologues are not limited to the canonical activity of Tpt1 healing the 2'-PO4, 3'-5' phosphodiester RNA splice junction formed during fungal and plant tRNA splicing [ (PUBMED:31019096) ]. Instead, the ADP-ribosyl transfer to a phosphorylated substrate is the unifying mechanistic feature of Tpt1-catalyzed reactions. For instance, some Tpt1 homologues have been shown to catalyze the transfer of ADP-ribose from NAD+ to a 5'-monophosphate end of RNA or DNA to install a 5'-phospho-ADP-ribose cap structure [ (PUBMED:30202863) ].
GO function:	NAD+ ADP-ribosyltransferase activity (GO:0003950)

PFAM accession number:

PF01885

Interpro abstract (IPR002745):

This entry includes Tpt1 and its homologues from all domains of life. Tpt1 was first discovered as an essential component of the fungal tRNA splicing pathway, which characteristically generates a 2'-PO4, 3'-5' phosphodiester splice junction during the tRNA ligation reaction [ (PUBMED:2154680) ]. It is an enzyme that catalyzes the transfer of an internal RNA 2'-monophosphate (2'-PO4) to NAD+ to form a 2'-OH RNA, ADP-ribose 1"-2" cyclic phosphate, and nicotinamide [ (PUBMED:8392224) ].

Interestingly, many Tpt1 homologues have no obvious need for an RNA 2'-phosphotransferase because: (i) they lack tRNA introns; and/or (ii) they are not known to have an enzymatic pathway that generates 2'-PO4, 3'-5' phosphodiester RNA structures. There are more evidence showing that Tpt1 homologues are not limited to the canonical activity of Tpt1 healing the 2'-PO4, 3'-5' phosphodiester RNA splice junction formed during fungal and plant tRNA splicing [ (PUBMED:31019096) ]. Instead, the ADP-ribosyl transfer to a phosphorylated substrate is the unifying mechanistic feature of Tpt1-catalyzed reactions. For instance, some Tpt1 homologues have been shown to catalyze the transfer of ADP-ribose from NAD+ to a 5'-monophosphate end of RNA or DNA to install a 5'-phospho-ADP-ribose cap structure [ (PUBMED:30202863) ].

GO function:

NAD+ ADP-ribosyltransferase activity (GO:0003950)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PTS_2-RNA