ID   I6TLE5_RIEAN            Unreviewed;       238 AA.
AC   I6TLE5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Aminoglycoside-3'-O-phosphotransferase {ECO:0000313|EMBL:AFM74299.1};
DE   Flags: Fragment;
GN   Name=aph {ECO:0000313|EMBL:AFM74299.1};
OS   Riemerella anatipestifer (Moraxella anatipestifer).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Riemerella.
OX   NCBI_TaxID=34085 {ECO:0000313|EMBL:AFM74299.1};
RN   [1] {ECO:0000313|EMBL:AFM74299.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GN3 {ECO:0000313|EMBL:AFM74299.1};
RX   PubMed=22445728; DOI=10.1016/j.vetmic.2012.02.027;
RA   Yang F.F., Sun Y.N., Li J.X., Wang H., Zhao M.J., Su J., Zhang Z.J.,
RA   Liu H.J., Jiang S.J.;
RT   "Detection of aminoglycoside resistance genes in Riemerella anatipestifer
RT   isolated from ducks.";
RL   Vet. Microbiol. 158:451-452(2012).
RN   [2] {ECO:0000313|EMBL:AFM74299.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GN3 {ECO:0000313|EMBL:AFM74299.1};
RA   Yang F., Jiang S.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
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DR   EMBL; JQ664657; AFM74299.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6TLE5; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd05150; APH; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR024165; Kan/Strep_kinase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Transferase {ECO:0000313|EMBL:AFM74299.1}.
FT   DOMAIN          8..235
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFM74299.1"
FT   NON_TER         238
FT                   /evidence="ECO:0000313|EMBL:AFM74299.1"
SQ   SEQUENCE   238 AA;  26066 MW;  27825A08E9CEB8E7 CRC64;
     DWAQQTIGCS DAAVFRLSAQ GRPVLFVKTD LSGALNELQD EAARLSWLAT TGVPCAAVLD
     VVTEAGRDWL LLGEVPGQDL LSSHLAPAEK VSIMADAMRR LHTLDPATCP FDHQAKHRIE
     RARTRMEAGL VDQDDLDEEH QGLAPAELFA RLKARMPDGE DLVVTHGDAC LPNIMVENGR
     FSGFIDCGRL GVADRYQDIA LATRDIAEEL GGEWADRFLV LYGIAAPDSQ RVAFYRLL
//