SMART: Pfam domain Thg1C

The domain within your query sequence starts at position 105 and ends at position 235; the E-value for the Thg1C domain shown below is 6.5e-54.

SNQTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQQRLKGTLTADKNEILFSEF
HINYNNEPHMYRKGTVLVWQKVEEVRTQEVRLPAEMEGEKKAVARTRTRVVALNCDLIGD
AFWKEHPEILA

Thg1C

PFAM accession number:	PF14413
Interpro abstract (IPR025845):	Thg1 was originally characterised as synthesising the guanine nucleotide at the -1 position of the histidinyl tRNA (HtRNA). Thg1 has also been shown to have polymerase activity, which has been proposed to be the ancestral activity of this enzyme [ (PUBMED:20080734) (PUBMED:16731615) ]. Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands [ (PUBMED:20591188) ]. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site [ (PUBMED:20591188) ]. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA [ (PUBMED:20591188) ].

PFAM accession number:

PF14413

Interpro abstract (IPR025845):

Thg1 was originally characterised as synthesising the guanine nucleotide at the -1 position of the histidinyl tRNA (HtRNA). Thg1 has also been shown to have polymerase activity, which has been proposed to be the ancestral activity of this enzyme [ (PUBMED:20080734) (PUBMED:16731615) ].

Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands [ (PUBMED:20591188) ]. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site [ (PUBMED:20591188) ]. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA [ (PUBMED:20591188) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Thg1C