SMART: Pfam domain 5

The domain within your query sequence starts at position 83 and ends at position 526; the E-value for the 5_nucleotid domain shown below is 1.8e-159.

IFSNNEMSLSDIEIYGFDYDYTLVFYSKHLHTLIFNAARDLLINEHRYPVEIRKYEYDPS
FAIRGLHYDVQRAVLMKIDAFHYIQMGTVYRGLSVVPDEEVIDMYEGSHVPLEQMSDFYG
KSSHGNTMKQFMDIFSLPEMTLLSCVNEHFLKNNIDYEPVHLYKDVKDSIRDVHIKGIMY
RAIEADIEKYICYADQTRAVLAKLAAHGKKMFLITNSPSSFVDKGMRYIVGKDWRDLFDV
VIVQAEKPNFFNDKRRPFRKVNEKGVLLWDKIHKLQKGQIYKQGNLYEFLKLTGWRGSKV
LYFGDHIYSDLADLTLKHGWRTGAIIPELRSELRIMNTEQYIQTMTWLQTLTGLLEQMQV
HRDAESQLVLQEWKKERKEMREMTKSFFNAQFGSLFRTDQNPTYFLRRLSRFADIYMASL
SCLLNYDVHHTFYPRRTPLQHELP

5_nucleotid

PFAM accession number:	PF05761
Interpro abstract (IPR008380):	This family includes a 5'-nucleotidase, EC 3.1.3.5 specific for purines (IMP and GMP) [ (PUBMED:9371705) ]. These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognised by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG", the domain appears to consist of a mixed alpha/beta fold.

PFAM accession number:

PF05761

Interpro abstract (IPR008380):

This family includes a 5'-nucleotidase, EC 3.1.3.5 specific for purines (IMP and GMP) [ (PUBMED:9371705) ]. These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognised by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG", the domain appears to consist of a mixed alpha/beta fold.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry 5_nucleotid