ID C5FJL6_ARTOC Unreviewed; 588 AA.
AC C5FJL6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aminoglycoside phosphotransferase domain-containing protein {ECO:0000259|Pfam:PF01636};
GN ORFNames=MCYG_03696 {ECO:0000313|EMBL:EEQ30877.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ30877.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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DR EMBL; DS995703; EEQ30877.1; -; Genomic_DNA.
DR RefSeq; XP_002848190.1; XM_002848144.1.
DR AlphaFoldDB; C5FJL6; -.
DR STRING; 554155.C5FJL6; -.
DR GeneID; 9229514; -.
DR VEuPathDB; FungiDB:MCYG_03696; -.
DR eggNOG; ENOG502SP9R; Eukaryota.
DR HOGENOM; CLU_037862_0_0_1; -.
DR OMA; WPEYWEF; -.
DR OrthoDB; 2251361at2759; -.
DR Proteomes; UP000002035; 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 Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR PANTHER; PTHR21310:SF56; APH DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT DOMAIN 359..552
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT REGION 278..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 66902 MW; FA38FCFEC18821E4 CRC64;
MDIPLATRLS QLQQALPAIY TKIGYHEMWG VDLVKGDPKL IETILTKFFI KASALHALII
ERTCMSIKDT LSWRKTVKPY PFPFKKMPEL SSFVHITLCK GHHVMWIKLD EEALKKYRLL
FEPLRYSGSI SNIVIGLLEA LMVVLLQSTS ISGDLKASFV VDCRPSNLPP LRLEKFGSFI
FNVRAALQSI QQHISSYYPG ILSRFYIINP FLEEFYKLKL PDDVLQKISI LQKKSELAKY
LGDGIPVQYG GSGRPLSEND CLSTQKLVDD HFLTHSNRGT IRDNNLTQPE AQKADPDSPK
PKGVQTHFSY SKIVGFPSTM LDPKDLDDWP DLCPGKGGAR VVHIDSGMLV KYGHGVRLAE
AEAMHLVATS TTVAVPRLIS AYILDDVCYI IMSFEEGKLL SSFWEHANEE EREKTVSSLK
DSVRQIRDIK GTYIGGLGQT SCRDPIFDAW WGDKPIEYGP FESESAFNEG IIQAMRNRFP
PNPRPIDPES PRHVSEYINH QTVRGLKGHQ IVFTHGDLRP DNIIVKPDCS VVFIDWGLSG
YRPEYWEYYR VMVTIPIKES WDLVVEKYIP PYYIETAIMR RIAAIMWN
//
