SMART: Pfam domain Cauli

The domain within your query sequence starts at position 27 and ends at position 70; the E-value for the Cauli_VI domain shown below is 4.4e-23.

MFYAVRRGRRTGVFLSWSECKAQVDRFPAARFKKFATEDEAWAF

Cauli_VI

PFAM accession number:	PF01693
Interpro abstract (IPR011320):	This entry represents the N-terminal domain of RNase HI, which has a 3-layer alpha/beta/alpha structure [ (PUBMED:10448044) ]. This domain is lacking in retroviral and prokaryotic enzymes, but shows a striking structural similarity to the ribosomal protein L9 N-terminal domain, and may function as a regulatory RNA-binding module. However, the topology of this domain differs from structures of known RNA binding domains such as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP motif. Eukaryotic RNases HI possess either one or two copies of this small N-terminal domain, in addition to the well-conserved catalytic RNase H domain. RNase HI belongs to the family of ribonuclease H enzymes that recognise RNA:DNA hybrids and degrade the RNA component.

PFAM accession number:

PF01693

Interpro abstract (IPR011320):

This entry represents the N-terminal domain of RNase HI, which has a 3-layer alpha/beta/alpha structure [ (PUBMED:10448044) ]. This domain is lacking in retroviral and prokaryotic enzymes, but shows a striking structural similarity to the ribosomal protein L9 N-terminal domain, and may function as a regulatory RNA-binding module. However, the topology of this domain differs from structures of known RNA binding domains such as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP motif. Eukaryotic RNases HI possess either one or two copies of this small N-terminal domain, in addition to the well-conserved catalytic RNase H domain. RNase HI belongs to the family of ribonuclease H enzymes that recognise RNA:DNA hybrids and degrade the RNA component.

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