ID A0A165F2S0_9APHY Unreviewed; 456 AA.
AC A0A165F2S0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Aminoglycoside phosphotransferase domain-containing protein {ECO:0000259|Pfam:PF01636};
GN ORFNames=LAESUDRAFT_676975 {ECO:0000313|EMBL:KZT08251.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT08251.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT08251.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT08251.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427616; KZT08251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F2S0; -.
DR STRING; 1314785.A0A165F2S0; -.
DR InParanoid; A0A165F2S0; -.
DR OrthoDB; 1659246at2759; -.
DR Proteomes; UP000076871; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR21310:SF59; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 283..330
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50885 MW; F55DF0B589FF3A80 CRC64;
MHSTINEDGR DNDCSTNCSA TTEVRRLDED KDALSNQEDE REGDEEEQLF AGIIAAIDIR
QLQAFVLAIR KETSPNLTDD VICTVYYPPH TGSYNIVYEV VFSDDVRWAI RIPAAGDVFS
PTFAQTMHLD IVAQRLVSSK TSMPLPHIHY WSVDAQNALG RPFMITDFVI GTNLSKVWND
SQWITDAKRE IIFKQLAWWM AELAELEFGQ IGRLEVDETS GTCVVVPFPE LSTLIVFADD
ETPPPVLGPA GPFISAHAFL SCVLYARRSL GDSPMLVMLQ LFLSVLPDPA LDGPPFVLGH
TDYDSQNIIV ADDGTITGII DWDGIYVGPR QGGAMAYPSW LTVDWDPLFY GWAENNSDEE
NGRFDSPTEL MKYRRAYLDA VDIASNGKLT QCTRNSHIWQ ALWIAITNEV ATAPIINRLS
KLLFGDEVLG YEIQTGISEG QWYRTGKGDI VELTAE
//
