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Database: UniProt
Entry: A0A1C4LUU9_9ACTN
LinkDB: A0A1C4LUU9_9ACTN
Original site: A0A1C4LUU9_9ACTN 
ID   A0A1C4LUU9_9ACTN        Unreviewed;       257 AA.
AC   A0A1C4LUU9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Kanamycin kinase {ECO:0000313|EMBL:SCD77303.1};
GN   ORFNames=GA0115240_12337 {ECO:0000313|EMBL:SCD77303.1};
OS   Streptomyces sp. DvalAA-14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCD77303.1, ECO:0000313|Proteomes:UP000199020};
RN   [1] {ECO:0000313|EMBL:SCD77303.1, ECO:0000313|Proteomes:UP000199020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCD77303.1,
RC   ECO:0000313|Proteomes:UP000199020};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
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DR   EMBL; FMCH01000219; SCD77303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4LUU9; -.
DR   OrthoDB; 3806873at2; -.
DR   Proteomes; UP000199020; Unassembled WGS sequence.
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; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW   ECO:0000256|PIRNR:PIRNR000706};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000706};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:SCD77303.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000706};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199020};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000706}.
FT   DOMAIN          47..250
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         202
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ   SEQUENCE   257 AA;  27327 MW;  FF97E51B9284B1AD CRC64;
     MLPPGRQHAG VRLSGPPDGE VPVPAPVAAL AGDRPLRPVW RNEAGGLTFQ LGGGPDRRFA
     KWAPAGSGLD LAAEAARLAW AGRFTTVPRV EARGADHGGA WLVTRGLPGD SAVSPRWLAD
     PRTAARALGE GLRALHDRLP VAGCPFSWSV GHRLERARRA GVELPADPPP PPPVDRLVVC
     HGDPCAPNTL LRADGSWSGH VDLGALGVAD RWADLAVATW STEWNYGPGW EDTLLDAYGV
     APDPERTAFY RRLWSAT
//
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