SMART: Pfam domain APH

The domain within your query sequence starts at position 108 and ends at position 358; the E-value for the APH domain shown below is 6.4e-12.

HISVIRGGLSNMLFQCSLPDSIASVGDEPRKVLLRLYGAILKMGAEAMVLESVMFAILAE
RSLGPKLFGIFPQGRLEQFIPSRRLDTEELRLPDISAEIAEKMATFHGMKMPFNKEPKWL
FGTMEKYLNQVLRLKFSREARVQQLHKILSYNLPLELENLRSLLQYTRSPVVFCHNDCQE
GNILLLEGQENSERRKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKY
PSRKQQLHFIS

APH

PFAM accession number:	PF01636
Interpro abstract (IPR002575):	This entry consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include:- aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation [ (PUBMED:2167474) ]. The proteins are found in a range of taxonomic groups.

PFAM accession number:

PF01636

Interpro abstract (IPR002575):

This entry consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include:- aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation [ (PUBMED:2167474) ]. The proteins are found in a range of taxonomic groups.

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