ID   G8PQP5_PSEUV            Unreviewed;       526 AA.
AC   G8PQP5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Protein containing Aminoglycoside phosphotransferase domain {ECO:0000313|EMBL:AEV35934.1};
GN   OrderedLocusNames=PSE_1422 {ECO:0000313|EMBL:AEV35934.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35934.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV35934.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35934.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003147; AEV35934.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8PQP5; -.
DR   STRING; 911045.PSE_1422; -.
DR   KEGG; psf:PSE_1422; -.
DR   eggNOG; COG0645; Bacteria.
DR   eggNOG; COG2187; Bacteria.
DR   HOGENOM; CLU_026771_1_0_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43883:SF1; GLUCONOKINASE; 1.
DR   PANTHER; PTHR43883; SLR0207 PROTEIN; 1.
DR   Pfam; PF13671; AAA_33; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000313|EMBL:AEV35934.1}.
FT   DOMAIN          134..289
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   526 AA;  58587 MW;  359B4F46B2B626E9 CRC64;
     MDGPMTADSF DVDTLTQSDI IGFFSSPDAH RGQEVKRIDT HANIAYLVGN DAYKMKRDVK
     FPFLDYSSLE KRKNACEAEI RLNSQYAPQI YRSTLPITLE RDGSLELAGH GDVVEWVVHM
     NRFNEHLGLD RVAEEKGISR ELALDLAKLM VDAHSRTTQR DAQPWIEDLL AYTNQNLDAF
     QEFPQFFPAD QVIALDKAAR EEHTFIESII LKRGEHGFVR LNHGDAHLAN IVMHDGKPLL
     FDAVEFDDAI ATGDVLYDLA FLLLDLCERN EPEAANVVLN AYLQQTHELK HLEDIRVLRF
     YLMMRAAIRA KIGAAASLHQ EGATRLKTEG QAQEYFRICQ RALAPTPPVL CVVGGLSGTG
     KTTLAQGLAP KLGRMPGAVH LRTDVIRKEM LEIGEADKAS KKTYTPEFSA KVYAELLRRA
     EMVLAAGHSV IIDGVYGKPA ERDSVEQLAK KTNAEFIGIW LEADVETLIN RVDARHGDAS
     DADAEVVRLQ QTYDLGEIHW AKLDSSKSKE AVLEQACSVT GLEPAL
//