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Database: UniProt
Entry: I0V1B4_9PSEU
LinkDB: I0V1B4_9PSEU
Original site: I0V1B4_9PSEU 
ID   I0V1B4_9PSEU            Unreviewed;       270 AA.
AC   I0V1B4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Aminoglycoside phosphotransferase {ECO:0000313|EMBL:EID53917.1};
GN   ORFNames=SacxiDRAFT_1674 {ECO:0000313|EMBL:EID53917.1};
OS   Saccharomonospora xinjiangensis XJ-54.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882086 {ECO:0000313|EMBL:EID53917.1, ECO:0000313|Proteomes:UP000004691};
RN   [1] {ECO:0000313|EMBL:EID53917.1, ECO:0000313|Proteomes:UP000004691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ-54 {ECO:0000313|EMBL:EID53917.1,
RC   ECO:0000313|Proteomes:UP000004691};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT   XJ-54.";
RL   Submitted (JAN-2012) 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; JH636049; EID53917.1; -; Genomic_DNA.
DR   RefSeq; WP_006238069.1; NZ_JH636049.1.
DR   AlphaFoldDB; I0V1B4; -.
DR   eggNOG; COG3231; Bacteria.
DR   HOGENOM; CLU_073027_2_0_11; -.
DR   OrthoDB; 3806873at2; -.
DR   Proteomes; UP000004691; 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; 1.
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};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000706};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:EID53917.1}.
FT   DOMAIN          51..262
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ   SEQUENCE   270 AA;  29221 MW;  7A0E18639F92A3E9 CRC64;
     MNTREVAEIP TGPVPVPSVV AELAKGDDIT PVWENELGGL TFRLDARIGG SRYVKWVAHG
     TPEIDLAAEA DRLAWASRWV RVPRVLGQGS NAEGSWLVTA PVPGRSAVDT RWLADPATAA
     TAIGHGLRVL HDALPVAECP YTWSVADRLA RADERIADGE GPGDWFPEHR HLTVAEARGL
     LDDAPPVDRL VVCHGDACAP NTLLHDDGTF AAHVDLGSLG VADRWADLAV AAWSTEWNHG
     PGYDHLVYAA YGVEPDPERI AYYRLLWDLA
//
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